3lx9: Difference between revisions

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New page: '''Unreleased structure''' The entry 3lx9 is ON HOLD Authors: Tomasic, I.B., Metcalf, M.C., Guce, A.I., Clark, N.E., Garman, S.C. Description: Interconversion of Human Lysosomal Enzyme...
 
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'''Unreleased structure'''


The entry 3lx9 is ON HOLD
==Interconversion of Human Lysosomal Enzyme Specificities==
<StructureSection load='3lx9' size='340' side='right'caption='[[3lx9]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3lx9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LX9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LX9 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.04&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3lx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lx9 OCA], [https://pdbe.org/3lx9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lx9 RCSB], [https://www.ebi.ac.uk/pdbsum/3lx9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lx9 ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/AGAL_HUMAN AGAL_HUMAN] Defects in GLA are the cause of Fabry disease (FD) [MIM:[https://omim.org/entry/301500 301500]. FD is a rare X-linked sphingolipidosis disease where glycolipid accumulates in many tissues. The disease consists of an inborn error of glycosphingolipid catabolism. FD patients show systemic accumulation of globotriaoslyceramide (Gb3) and related glycosphingolipids in the plasma and cellular lysosomes throughout the body. Clinical recognition in males results from characteristic skin lesions (angiokeratomas) over the lower trunk. Patients may show ocular deposits, febrile episodes, and burning pain in the extremities. Death results from renal failure, cardiac or cerebral complications of hypertension or other vascular disease. Heterozygous females may exhibit the disorder in an attenuated form, they are more likely to show corneal opacities.<ref>PMID:2152885</ref> <ref>PMID:1846223</ref> <ref>PMID:2171331</ref> <ref>PMID:2539398</ref> <ref>PMID:1315715</ref> <ref>PMID:7504405</ref> <ref>PMID:8395937</ref> <ref>PMID:8069316</ref> <ref>PMID:7531540</ref> <ref>PMID:7575533</ref> <ref>PMID:7759078</ref> <ref>PMID:7599642</ref> <ref>PMID:7596372</ref> <ref>PMID:8738659</ref> <ref>PMID:8875188</ref> <ref>PMID:8834244</ref> <ref>PMID:8931708</ref> <ref>PMID:8807334</ref> <ref>PMID:8863162</ref> <ref>PMID:9105656</ref> <ref>PMID:9100224</ref> <ref>PMID:9554750</ref> <ref>PMID:9452068</ref> <ref>PMID:9452090</ref> <ref>PMID:9452111</ref> <ref>PMID:10208848</ref> <ref>PMID:10090526</ref> <ref>PMID:10838196</ref> <ref>PMID:10666480</ref> <ref>PMID:11076046</ref> <ref>PMID:10916280</ref> <ref>PMID:11295840</ref> <ref>PMID:11668641</ref> <ref>PMID:11889412</ref> <ref>PMID:12694230</ref> <ref>PMID:12786754</ref> <ref>PMID:15162124</ref> <ref>PMID:15712228</ref> <ref>PMID:16533976</ref> <ref>PMID:19621417</ref>
== Function ==
[https://www.uniprot.org/uniprot/AGAL_HUMAN AGAL_HUMAN]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lx/3lx9_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lx9 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The human lysosomal enzymes alpha-galactosidase (alpha-GAL, EC 3.2.1.22) and alpha-N-acetylgalactosaminidase (alpha-NAGAL, EC 3.2.1.49) share 46% amino acid sequence identity and have similar folds. The active sites of the two enzymes share 11 of 13 amino acids, differing only where they interact with the 2-position of the substrates. Using a rational protein engineering approach, we interconverted the enzymatic specificity of alpha- GAL and alpha-NAGAL. The engineered alpha-GAL (which we call alpha-GAL(SA)) retains the antigenicity of alpha-GAL but has acquired the enzymatic specificity of alpha-NAGAL. Conversely, the engineered alpha-NAGAL (which we call alpha-NAGAL(EL)) retains the antigenicity of alpha-NAGAL but has acquired the enzymatic specificity of the alpha-GAL enzyme. Comparison of the crystal structures of the designed enzyme alpha-GAL(SA) to the wild-type enzymes shows that active sites of alpha-GAL(SA) and alpha-NAGAL superimpose well, indicating success of the rational design. The designed enzymes might be useful as non-immunogenic alternatives in enzyme replacement therapy for treatment of lysosomal storage disorders such as Fabry disease.


Authors: Tomasic, I.B., Metcalf, M.C., Guce, A.I., Clark, N.E., Garman, S.C.
Interconversion of the specificities of human lysosomal enzymes associated with Fabry and Schindler diseases.,Tomasic IB, Metcalf MC, Guce AI, Clark NE, Garman SC J Biol Chem. 2010 Jul 9;285(28):21560-6. Epub 2010 May 5. PMID:20444686<ref>PMID:20444686</ref>


Description: Interconversion of Human Lysosomal Enzyme Specificities
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3lx9" style="background-color:#fffaf0;"></div>


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar  3 15:30:56 2010''
==See Also==
*[[Galactosidase 3D structures|Galactosidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Clark NE]]
[[Category: Garman SC]]
[[Category: Guce AI]]
[[Category: Metcalf MC]]
[[Category: Tomasic IB]]

Latest revision as of 05:06, 21 November 2024

Interconversion of Human Lysosomal Enzyme SpecificitiesInterconversion of Human Lysosomal Enzyme Specificities

Structural highlights

3lx9 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.04Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

AGAL_HUMAN Defects in GLA are the cause of Fabry disease (FD) [MIM:301500. FD is a rare X-linked sphingolipidosis disease where glycolipid accumulates in many tissues. The disease consists of an inborn error of glycosphingolipid catabolism. FD patients show systemic accumulation of globotriaoslyceramide (Gb3) and related glycosphingolipids in the plasma and cellular lysosomes throughout the body. Clinical recognition in males results from characteristic skin lesions (angiokeratomas) over the lower trunk. Patients may show ocular deposits, febrile episodes, and burning pain in the extremities. Death results from renal failure, cardiac or cerebral complications of hypertension or other vascular disease. Heterozygous females may exhibit the disorder in an attenuated form, they are more likely to show corneal opacities.[1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11] [12] [13] [14] [15] [16] [17] [18] [19] [20] [21] [22] [23] [24] [25] [26] [27] [28] [29] [30] [31] [32] [33] [34] [35] [36] [37] [38] [39] [40]

Function

AGAL_HUMAN

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The human lysosomal enzymes alpha-galactosidase (alpha-GAL, EC 3.2.1.22) and alpha-N-acetylgalactosaminidase (alpha-NAGAL, EC 3.2.1.49) share 46% amino acid sequence identity and have similar folds. The active sites of the two enzymes share 11 of 13 amino acids, differing only where they interact with the 2-position of the substrates. Using a rational protein engineering approach, we interconverted the enzymatic specificity of alpha- GAL and alpha-NAGAL. The engineered alpha-GAL (which we call alpha-GAL(SA)) retains the antigenicity of alpha-GAL but has acquired the enzymatic specificity of alpha-NAGAL. Conversely, the engineered alpha-NAGAL (which we call alpha-NAGAL(EL)) retains the antigenicity of alpha-NAGAL but has acquired the enzymatic specificity of the alpha-GAL enzyme. Comparison of the crystal structures of the designed enzyme alpha-GAL(SA) to the wild-type enzymes shows that active sites of alpha-GAL(SA) and alpha-NAGAL superimpose well, indicating success of the rational design. The designed enzymes might be useful as non-immunogenic alternatives in enzyme replacement therapy for treatment of lysosomal storage disorders such as Fabry disease.

Interconversion of the specificities of human lysosomal enzymes associated with Fabry and Schindler diseases.,Tomasic IB, Metcalf MC, Guce AI, Clark NE, Garman SC J Biol Chem. 2010 Jul 9;285(28):21560-6. Epub 2010 May 5. PMID:20444686[41]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Koide T, Ishiura M, Iwai K, Inoue M, Kaneda Y, Okada Y, Uchida T. A case of Fabry's disease in a patient with no alpha-galactosidase A activity caused by a single amino acid substitution of Pro-40 by Ser. FEBS Lett. 1990 Jan 1;259(2):353-6. PMID:2152885
  2. ↑ von Scheidt W, Eng CM, Fitzmaurice TF, Erdmann E, Hubner G, Olsen EG, Christomanou H, Kandolf R, Bishop DF, Desnick RJ. An atypical variant of Fabry's disease with manifestations confined to the myocardium. N Engl J Med. 1991 Feb 7;324(6):395-9. PMID:1846223 doi:http://dx.doi.org/10.1056/NEJM199102073240607
  3. ↑ Sakuraba H, Oshima A, Fukuhara Y, Shimmoto M, Nagao Y, Bishop DF, Desnick RJ, Suzuki Y. Identification of point mutations in the alpha-galactosidase A gene in classical and atypical hemizygotes with Fabry disease. Am J Hum Genet. 1990 Nov;47(5):784-9. PMID:2171331
  4. ↑ Bernstein HS, Bishop DF, Astrin KH, Kornreich R, Eng CM, Sakuraba H, Desnick RJ. Fabry disease: six gene rearrangements and an exonic point mutation in the alpha-galactosidase gene. J Clin Invest. 1989 Apr;83(4):1390-9. PMID:2539398 doi:http://dx.doi.org/10.1172/JCI114027
  5. ↑ Ishii S, Sakuraba H, Suzuki Y. Point mutations in the upstream region of the alpha-galactosidase A gene exon 6 in an atypical variant of Fabry disease. Hum Genet. 1992 Apr;89(1):29-32. PMID:1315715
  6. ↑ Eng CM, Resnick-Silverman LA, Niehaus DJ, Astrin KH, Desnick RJ. Nature and frequency of mutations in the alpha-galactosidase A gene that cause Fabry disease. Am J Hum Genet. 1993 Dec;53(6):1186-97. PMID:7504405
  7. ↑ Davies JP, Winchester BG, Malcolm S. Mutation analysis in patients with the typical form of Anderson-Fabry disease. Hum Mol Genet. 1993 Jul;2(7):1051-3. PMID:8395937
  8. ↑ Davies J, Christomanou H, Winchester B, Malcolm S. Detection of 8 new mutations in the alpha-galactosidase A gene in Fabry disease. Hum Mol Genet. 1994 Apr;3(4):667-9. PMID:8069316
  9. ↑ Eng CM, Niehaus DJ, Enriquez AL, Burgert TS, Ludman MD, Desnick RJ. Fabry disease: twenty-three mutations including sense and antisense CpG alterations and identification of a deletional hot-spot in the alpha-galactosidase A gene. Hum Mol Genet. 1994 Oct;3(10):1795-9. PMID:7531540
  10. ↑ Okumiya T, Ishii S, Takenaka T, Kase R, Kamei S, Sakuraba H, Suzuki Y. Galactose stabilizes various missense mutants of alpha-galactosidase in Fabry disease. Biochem Biophys Res Commun. 1995 Sep 25;214(3):1219-24. PMID:7575533 doi:http://dx.doi.org/10.1006/bbrc.1995.2416
  11. ↑ Okumiya T, Ishii S, Kase R, Kamei S, Sakuraba H, Suzuki Y. Alpha-galactosidase gene mutations in Fabry disease: heterogeneous expressions of mutant enzyme proteins. Hum Genet. 1995 May;95(5):557-61. PMID:7759078
  12. ↑ Madsen KM, Hasholt L, Sorensen SA, Fermer ML, Dahl N. Two novel mutations (L32P) and (G85N) among five different missense mutations in six Danish families with Fabry's disease. Hum Mutat. 1995;5(3):277-8. PMID:7599642 doi:http://dx.doi.org/10.1002/humu.1380050316
  13. ↑ Nakao S, Takenaka T, Maeda M, Kodama C, Tanaka A, Tahara M, Yoshida A, Kuriyama M, Hayashibe H, Sakuraba H, et al.. An atypical variant of Fabry's disease in men with left ventricular hypertrophy. N Engl J Med. 1995 Aug 3;333(5):288-93. PMID:7596372 doi:http://dx.doi.org/10.1056/NEJM199508033330504
  14. ↑ Sawada K, Mizoguchi K, Hishida A, Kaneko E, Koide Y, Nishimura K, Kimura M. Point mutation in the alpha-galactosidase A gene of atypical Fabry disease with only nephropathy. Clin Nephrol. 1996 May;45(5):289-94. PMID:8738659
  15. ↑ Davies JP, Eng CM, Hill JA, Malcolm S, MacDermot K, Winchester B, Desnick RJ. Fabry disease: fourteen alpha-galactosidase A mutations in unrelated families from the United Kingdom and other European countries. Eur J Hum Genet. 1996;4(4):219-24. PMID:8875188
  16. ↑ Cariolou MA, Christodoulides M, Manoli P, Kokkofitou A, Tsambaos D. Novel trinucleotide deletion in Fabry's disease. Hum Genet. 1996 Apr;97(4):468-70. PMID:8834244
  17. ↑ Germain D, Biasotto M, Tosi M, Meo T, Kahn A, Poenaru L. Fluorescence-assisted mismatch analysis (FAMA) for exhaustive screening of the alpha-galactosidase A gene and detection of carriers in Fabry disease. Hum Genet. 1996 Dec;98(6):719-26. PMID:8931708
  18. ↑ Blanch LC, Meaney C, Morris CP. A sensitive mutation screening strategy for Fabry disease: detection of nine mutations in the alpha-galactosidase A gene. Hum Mutat. 1996;8(1):38-43. PMID:8807334 doi:<38::AID-HUMU5>3.0.CO;2-L 10.1002/(SICI)1098-1004(1996)8:1<38::AID-HUMU5>3.0.CO;2-L
  19. ↑ Redonnet-Vernhet I, Ploos van Amstel JK, Jansen RP, Wevers RA, Salvayre R, Levade T. Uneven X inactivation in a female monozygotic twin pair with Fabry disease and discordant expression of a novel mutation in the alpha-galactosidase A gene. J Med Genet. 1996 Aug;33(8):682-8. PMID:8863162
  20. ↑ Takata T, Okumiya T, Hayashibe H, Shimmoto M, Kase R, Itoh K, Utsumi K, Kamei S, Sakuraba H. Screening and detection of gene mutations in Japanese patients with Fabry disease by non-radioactive single-stranded conformation polymorphism analysis. Brain Dev. 1997 Mar;19(2):111-6. PMID:9105656
  21. ↑ Eng CM, Ashley GA, Burgert TS, Enriquez AL, D'Souza M, Desnick RJ. Fabry disease: thirty-five mutations in the alpha-galactosidase A gene in patients with classic and variant phenotypes. Mol Med. 1997 Mar;3(3):174-82. PMID:9100224
  22. ↑ Chen CH, Shyu PW, Wu SJ, Sheu SS, Desnick RJ, Hsiao KJ. Identification of a novel point mutation (S65T) in alpha-galactosidase A gene in Chinese patients with Fabry disease. Mutations in brief no. 169. Online. Hum Mutat. 1998;11(4):328-30. PMID:9554750 doi:<328::AID-HUMU11>3.0.CO;2-N 10.1002/(SICI)1098-1004(1998)11:4<328::AID-HUMU11>3.0.CO;2-N
  23. ↑ Miyazaki T, Kajita M, Ohmori S, Mizutani N, Niwa T, Murata Y, Seo H. A novel mutation (E358K) in the alpha-galactosidase A gene detected in a Japanese family with Fabry disease. Hum Mutat. 1998;Suppl 1:S139-40. PMID:9452068
  24. ↑ Okumiya T, Kawamura O, Itoh K, Kase R, Ishii S, Kamei S, Sakuraba H. Novel missense mutation (M72V) of alpha-galactosidase gene and its expression product in an atypical Fabry hemizygote. Hum Mutat. 1998;Suppl 1:S213-6. PMID:9452090
  25. ↑ Guffon N, Froissart R, Chevalier-Porst F, Maire I. Mutation analysis in 11 French patients with Fabry disease. Hum Mutat. 1998;Suppl 1:S288-90. PMID:9452111
  26. ↑ Germain DP, Poenaru L. Fabry disease: identification of novel alpha-galactosidase A mutations and molecular carrier detection by use of fluorescent chemical cleavage of mismatches. Biochem Biophys Res Commun. 1999 Apr 21;257(3):708-13. PMID:10208848 doi:10.1006/bbrc.1999.0310
  27. ↑ Beyer EM, Karpova EA, Udalova OV, Ploos van Amstel JK, van Diggelen OP, Tsvetkova IV. The multiple cases of Fabry disease in a Russian family caused by an E341K amino acid substitution in the alpha-galactosidase A. Clin Chim Acta. 1999 Feb;280(1-2):81-9. PMID:10090526
  28. ↑ Kase R, Bierfreund U, Klein A, Kolter T, Utsumi K, Itoha K, Sandhoff K, Sakuraba H. Characterization of two alpha-galactosidase mutants (Q279E and R301Q) found in an atypical variant of Fabry disease. Biochim Biophys Acta. 2000 Jun 15;1501(2-3):227-35. PMID:10838196
  29. ↑ Topaloglu AK, Ashley GA, Tong B, Shabbeer J, Astrin KH, Eng CM, Desnick RJ. Twenty novel mutations in the alpha-galactosidase A gene causing Fabry disease. Mol Med. 1999 Dec;5(12):806-11. PMID:10666480
  30. ↑ Lee JK, Kim GH, Kim JS, Kim KK, Lee MC, Yoo HW. Identification of four novel mutations in five unrelated Korean families with Fabry disease. Clin Genet. 2000 Sep;58(3):228-33. PMID:11076046
  31. ↑ Ashton-Prolla P, Tong B, Shabbeer J, Astrin KH, Eng CM, Desnick RJ. Fabry disease: twenty-two novel mutations in the alpha-galactosidase A gene and genotype/phenotype correlations in severely and mildly affected hemizygotes and heterozygotes. J Investig Med. 2000 Jul;48(4):227-35. PMID:10916280
  32. ↑ Germain DP, Salard D, Fellmann F, Azibi K, Caillaud C, Bernard MC, Poenaru L. Identification of a novel de novo mutation (G373D) in the alpha-galactosidase A gene (GLA) in a patient affected with Fabry disease. Hum Mutat. 2001 Apr;17(4):353. PMID:11295840 doi:10.1002/humu.41
  33. ↑ Blaydon D, Hill J, Winchester B. Fabry disease: 20 novel GLA mutations in 35 families. Hum Mutat. 2001 Nov;18(5):459. PMID:11668641 doi:10.1002/humu.1219
  34. ↑ Branton MH, Schiffmann R, Sabnis SG, Murray GJ, Quirk JM, Altarescu G, Goldfarb L, Brady RO, Balow JE, Austin Iii HA, Kopp JB. Natural history of Fabry renal disease: influence of alpha-galactosidase A activity and genetic mutations on clinical course. Medicine (Baltimore). 2002 Mar;81(2):122-38. PMID:11889412
  35. ↑ Yang CC, Lai LW, Whitehair O, Hwu WL, Chiang SC, Lien YH. Two novel mutations in the alpha-galactosidase A gene in Chinese patients with Fabry disease. Clin Genet. 2003 Mar;63(3):205-9. PMID:12694230
  36. ↑ Lai LW, Whitehair O, Wu MJ, O'Meara M, Lien YH. Analysis of splice-site mutations of the alpha-galactosidase A gene in Fabry disease. Clin Genet. 2003 Jun;63(6):476-82. PMID:12786754
  37. ↑ Verovnik F, Benko D, Vujkovac B, Linthorst GE. Remarkable variability in renal disease in a large Slovenian family with Fabry disease. Eur J Hum Genet. 2004 Aug;12(8):678-81. PMID:15162124 doi:10.1038/sj.ejhg.5201184
  38. ↑ Shabbeer J, Robinson M, Desnick RJ. Detection of alpha-galactosidase a mutations causing Fabry disease by denaturing high performance liquid chromatography. Hum Mutat. 2005 Mar;25(3):299-305. PMID:15712228 doi:10.1002/humu.20144
  39. ↑ Nance CS, Klein CJ, Banikazemi M, Dikman SH, Phelps RG, McArthur JC, Rodriguez M, Desnick RJ. Later-onset Fabry disease: an adult variant presenting with the cramp-fasciculation syndrome. Arch Neurol. 2006 Mar;63(3):453-7. PMID:16533976 doi:63/3/453
  40. ↑ Hwu WL, Chien YH, Lee NC, Chiang SC, Dobrovolny R, Huang AC, Yeh HY, Chao MC, Lin SJ, Kitagawa T, Desnick RJ, Hsu LW. Newborn screening for Fabry disease in Taiwan reveals a high incidence of the later-onset GLA mutation c.936+919G>A (IVS4+919G>A). Hum Mutat. 2009 Oct;30(10):1397-405. doi: 10.1002/humu.21074. PMID:19621417 doi:10.1002/humu.21074
  41. ↑ Tomasic IB, Metcalf MC, Guce AI, Clark NE, Garman SC. Interconversion of the specificities of human lysosomal enzymes associated with Fabry and Schindler diseases. J Biol Chem. 2010 Jul 9;285(28):21560-6. Epub 2010 May 5. PMID:20444686 doi:10.1074/jbc.M110.118588

3lx9, resolution 2.04Å

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