2xw0: Difference between revisions

Revision as of 23:32, 4 August 2016

HUMAN SERUM ALBUMIN COMPLEXED WITH DANSYL-L-PHENYLALANINEHUMAN SERUM ALBUMIN COMPLEXED WITH DANSYL-L-PHENYLALANINE

Structural highlights

2xw0 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2bxq, 1hk4, 2xvu, 2bxi, 2vuf, 2xvv, 1o9x, 1bke, 2bxk, 1hk1, 1uor, 1h9z, 1e7b, 1hk2, 1hk5, 2esg, 1e7e, 2xvq, 2bxg, 2bxh, 2bxo, 2bxf, 1ysx, 1e7g, 1ao6, 2bxc, 1tf0, 2bxn, 2bxe, 1e7c, 1gnj, 1e7h, 2bxa, 1hk3, 2xvw, 2xw1, 1e7i, 2bxb, 2bxl, 1gni, 1ha2, 1bj5, 1e7a, 2bxp, 1bm0, 2bxd, 1e78, 2vdb, 1e7f, 1n5u, 2bx8, 2bxm, 2vue
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[ALBU_HUMAN] Defects in ALB are a cause of familial dysalbuminemic hyperthyroxinemia (FDH) [MIM:103600]. FDH is a form of euthyroid hyperthyroxinemia that is due to increased affinity of ALB for T(4). It is the most common cause of inherited euthyroid hyperthyroxinemia in Caucasian population.^[1] ^[2] ^[3] ^[4]

Function

[ALBU_HUMAN] Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc.^[5]

Publication Abstract from PubMed

Human serum albumin (HSA) has two primary binding sites for drug molecules. These sites selectively bind different dansylated amino acid compounds, which-due to their intrinsic fluorescence-have long been used as specific markers for the drug pockets on HSA. We present here the co-crystal structures of HSA in complex with six dansylated amino acids that are specific for either drug site 1 (dansyl-l-asparagine, dansyl-l-arginine, dansyl-l-glutamate) or drug site 2 (dansyl-l-norvaline, dansyl-l-phenylalanine, dansyl-l-sarcosine). Our results explain the structural basis of the site-specificity of different dansylated amino acids. They also show that fatty acid binding has only a modest effect on binding of dansylated amino acids to drug site 1 and identify the location of secondary binding sites.

Structural basis of binding of fluorescent, site-specific dansylated amino acids to human serum albumin.,Ryan AJ, Ghuman J, Zunszain PA, Chung CW, Curry S J Struct Biol. 2010 Oct 18. PMID:20940056^[6]

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

References

↑ Sunthornthepvarakul T, Angkeow P, Weiss RE, Hayashi Y, Refetoff S. An identical missense mutation in the albumin gene results in familial dysalbuminemic hyperthyroxinemia in 8 unrelated families. Biochem Biophys Res Commun. 1994 Jul 29;202(2):781-7. PMID:8048949
↑ Rushbrook JI, Becker E, Schussler GC, Divino CM. Identification of a human serum albumin species associated with familial dysalbuminemic hyperthyroxinemia. J Clin Endocrinol Metab. 1995 Feb;80(2):461-7. PMID:7852505
↑ Wada N, Chiba H, Shimizu C, Kijima H, Kubo M, Koike T. A novel missense mutation in codon 218 of the albumin gene in a distinct phenotype of familial dysalbuminemic hyperthyroxinemia in a Japanese kindred. J Clin Endocrinol Metab. 1997 Oct;82(10):3246-50. PMID:9329347
↑ Sunthornthepvarakul T, Likitmaskul S, Ngowngarmratana S, Angsusingha K, Kitvitayasak S, Scherberg NH, Refetoff S. Familial dysalbuminemic hypertriiodothyroninemia: a new, dominantly inherited albumin defect. J Clin Endocrinol Metab. 1998 May;83(5):1448-54. PMID:9589637
↑ Lu J, Stewart AJ, Sadler PJ, Pinheiro TJ, Blindauer CA. Albumin as a zinc carrier: properties of its high-affinity zinc-binding site. Biochem Soc Trans. 2008 Dec;36(Pt 6):1317-21. doi: 10.1042/BST0361317. PMID:19021548 doi:10.1042/BST0361317
↑ Ryan AJ, Ghuman J, Zunszain PA, Chung CW, Curry S. Structural basis of binding of fluorescent, site-specific dansylated amino acids to human serum albumin. J Struct Biol. 2010 Oct 18. PMID:20940056 doi:10.1016/j.jsb.2010.10.004

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OCA

[1] Sunthornthepvarakul T, Angkeow P, Weiss RE, Hayashi Y, Refetoff S. An identical missense mutation in the albumin gene results in familial dysalbuminemic hyperthyroxinemia in 8 unrelated families. Biochem Biophys Res Commun. 1994 Jul 29;202(2):781-7. PMID:8048949

[2] Rushbrook JI, Becker E, Schussler GC, Divino CM. Identification of a human serum albumin species associated with familial dysalbuminemic hyperthyroxinemia. J Clin Endocrinol Metab. 1995 Feb;80(2):461-7. PMID:7852505

[3] Wada N, Chiba H, Shimizu C, Kijima H, Kubo M, Koike T. A novel missense mutation in codon 218 of the albumin gene in a distinct phenotype of familial dysalbuminemic hyperthyroxinemia in a Japanese kindred. J Clin Endocrinol Metab. 1997 Oct;82(10):3246-50. PMID:9329347

[4] Sunthornthepvarakul T, Likitmaskul S, Ngowngarmratana S, Angsusingha K, Kitvitayasak S, Scherberg NH, Refetoff S. Familial dysalbuminemic hypertriiodothyroninemia: a new, dominantly inherited albumin defect. J Clin Endocrinol Metab. 1998 May;83(5):1448-54. PMID:9589637

[5] Lu J, Stewart AJ, Sadler PJ, Pinheiro TJ, Blindauer CA. Albumin as a zinc carrier: properties of its high-affinity zinc-binding site. Biochem Soc Trans. 2008 Dec;36(Pt 6):1317-21. doi: 10.1042/BST0361317. PMID:19021548 doi:10.1042/BST0361317

[6] Ryan AJ, Ghuman J, Zunszain PA, Chung CW, Curry S. Structural basis of binding of fluorescent, site-specific dansylated amino acids to human serum albumin. J Struct Biol. 2010 Oct 18. PMID:20940056 doi:10.1016/j.jsb.2010.10.004

[1]

[2]

[3]

[4]

[5]

[6]

@@ Line 1: / Line 1: @@
 ==HUMAN SERUM ALBUMIN COMPLEXED WITH DANSYL-L-PHENYLALANINE==
 <StructureSection load='2xw0' size='340' side='right' caption='[[2xw0]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2xw0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XW0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XW0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2xw0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XW0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XW0 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=9NF:DANSYL-L-PHENYLALANINE'>9NF</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bxq|2bxq]], [[1hk4|1hk4]], [[2xvu|2xvu]], [[2bxi|2bxi]], [[2vuf|2vuf]], [[2xvv|2xvv]], [[1o9x|1o9x]], [[1bke|1bke]], [[2bxk|2bxk]], [[1hk1|1hk1]], [[1uor|1uor]], [[1h9z|1h9z]], [[1e7b|1e7b]], [[1hk2|1hk2]], [[1hk5|1hk5]], [[2esg|2esg]], [[1e7e|1e7e]], [[2xvq|2xvq]], [[2bxg|2bxg]], [[2bxh|2bxh]], [[2bxo|2bxo]], [[2bxf|2bxf]], [[1ysx|1ysx]], [[1e7g|1e7g]], [[1ao6|1ao6]], [[2bxc|2bxc]], [[1tf0|1tf0]], [[2bxn|2bxn]], [[2bxe|2bxe]], [[1e7c|1e7c]], [[1gnj|1gnj]], [[1e7h|1e7h]], [[2bxa|2bxa]], [[1hk3|1hk3]], [[2xvw|2xvw]], [[2xw1|2xw1]], [[1e7i|1e7i]], [[2bxb|2bxb]], [[2bxl|2bxl]], [[1gni|1gni]], [[1ha2|1ha2]], [[1bj5|1bj5]], [[1e7a|1e7a]], [[2bxp|2bxp]], [[1bm0|1bm0]], [[2bxd|2bxd]], [[1e78|1e78]], [[2vdb|2vdb]], [[1e7f|1e7f]], [[1n5u|1n5u]], [[2bx8|2bx8]], [[2bxm|2bxm]], [[2vue|2vue]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xw0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xw0 RCSB], [http://www.ebi.ac.uk/pdbsum/2xw0 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xw0 OCA], [http://pdbe.org/2xw0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xw0 RCSB], [http://www.ebi.ac.uk/pdbsum/2xw0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xw0 ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 19: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2xw0" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 26: / Line 28: @@
 __TOC__
 </StructureSection>
-[[Category: Homo sapiens]]
+[[Category: Human]]
 [[Category: Curry, S]]
 [[Category: Ryan, A J]]
 [[Category: Transport protein]]

2xw0: Difference between revisions

Revision as of 23:32, 4 August 2016

HUMAN SERUM ALBUMIN COMPLEXED WITH DANSYL-L-PHENYLALANINEHUMAN SERUM ALBUMIN COMPLEXED WITH DANSYL-L-PHENYLALANINE

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

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2xw0: Difference between revisions

Revision as of 23:32, 4 August 2016

HUMAN SERUM ALBUMIN COMPLEXED WITH DANSYL-L-PHENYLALANINEHUMAN SERUM ALBUMIN COMPLEXED WITH DANSYL-L-PHENYLALANINE

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

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