3cyu: Difference between revisions

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==Human Carbonic Anhydrase II complexed with Cryptophane biosensor and xenon==
The line below this paragraph, containing "STRUCTURE_3cyu", creates the "Structure Box" on the page.
<StructureSection load='3cyu' size='340' side='right'caption='[[3cyu]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3cyu]] is a 1 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=3CYU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CYU FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0CR:MOMO-2-[4-(2-(4-(METHOXY)-1H-1,2,3-TRIAZOL-1-YL)ETHYL)BENZENESULFONAMIDE]-7,12-BIS-[3-(4-(METHOXY)-1H-1,2,3-TRIAZOL-1-YL)PROPANOIC+ACID]-CRYPTOPHANE-A'>0CR</scene>, <scene name='pdbligand=1CR:POPO-2-[4-(2-(4-(METHOXY)-1H-1,2,3-TRIAZOL-1-YL)ETHYL)BENZENESULFONAMIDE]-7,12-BIS-[3-(4-(METHOXY)-1H-1,2,3-TRIAZOL-1-YL)PROPANOIC+ACID]-CRYPTOPHANE-A'>1CR</scene>, <scene name='pdbligand=XE:XENON'>XE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
{{STRUCTURE_3cyu|  PDB=3cyu  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3cyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cyu OCA], [https://pdbe.org/3cyu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cyu RCSB], [https://www.ebi.ac.uk/pdbsum/3cyu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cyu ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/CAH2_HUMAN CAH2_HUMAN] Defects in CA2 are the cause of osteopetrosis autosomal recessive type 3 (OPTB3) [MIM:[https://omim.org/entry/259730 259730]; also known as osteopetrosis with renal tubular acidosis, carbonic anhydrase II deficiency syndrome, Guibaud-Vainsel syndrome or marble brain disease. Osteopetrosis is a rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. The disorder occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Autosomal recessive osteopetrosis is usually associated with normal or elevated amount of non-functional osteoclasts. OPTB3 is associated with renal tubular acidosis, cerebral calcification (marble brain disease) and in some cases with mental retardation.<ref>PMID:1928091</ref> <ref>PMID:1542674</ref> <ref>PMID:8834238</ref> <ref>PMID:9143915</ref> <ref>PMID:15300855</ref>
== Function ==
[https://www.uniprot.org/uniprot/CAH2_HUMAN CAH2_HUMAN] Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide. Can hydrate cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye.<ref>PMID:10550681</ref> <ref>PMID:11831900</ref>
== 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/cy/3cyu_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=3cyu ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cryptophanes represent an exciting class of xenon-encapsulating molecules that can be exploited as probes for nuclear magnetic resonance imaging. The 1.70 A resolution crystal structure of a cryptophane-derivatized benezenesulfonamide complexed with human carbonic anhydrase II shows how an encapsulated xenon atom can be directed to a specific biological target. The crystal structure confirms binding measurements indicating that the cryptophane cage does not strongly interact with the surface of the protein, which may enhance the sensitivity of 129Xe NMR spectroscopic measurements in solution.


'''Human Carbonic Anhydrase II complexed with Cryptophane biosensor and xenon'''
Structure of a 129Xe-cryptophane biosensor complexed with human carbonic anhydrase II.,Aaron JA, Chambers JM, Jude KM, Di Costanzo L, Dmochowski IJ, Christianson DW J Am Chem Soc. 2008 Jun 4;130(22):6942-3. Epub 2008 May 8. PMID:18461940<ref>PMID:18461940</ref>


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


==Disease==
==See Also==
Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=611492 611492]]
*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
 
== References ==
==About this Structure==
<references/>
3CYU is a [[Single protein]] structure of 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=3CYU OCA].
__TOC__
 
</StructureSection>
==Reference==
Structure of a (129)Xe-Cryptophane Biosensor Complexed with Human Carbonic Anhydrase II., Aaron JA, Chambers JM, Jude KM, Di Costanzo L, Dmochowski IJ, Christianson DW, J Am Chem Soc. 2008 May 8;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18461940 18461940]
[[Category: Carbonate dehydratase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Aaron, J A.]]
[[Category: Aaron JA]]
[[Category: Christianson, D W.]]
[[Category: Christianson DW]]
[[Category: Costanzo, L Di.]]
[[Category: Di Costanzo L]]
[[Category: Jude, K M.]]
[[Category: Jude KM]]
[[Category: Acetylation]]
[[Category: Biosensor]]
[[Category: Cryptophane]]
[[Category: Cytoplasm]]
[[Category: Disease mutation]]
[[Category: Lyase]]
[[Category: Metal-binding]]
[[Category: Polymorphism]]
[[Category: Sulfonamide]]
[[Category: Xenon]]
[[Category: Zinc]]
[[Category: Zinc metalloenzyme]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 28 09:24:41 2008''

Latest revision as of 15:35, 30 August 2023

Human Carbonic Anhydrase II complexed with Cryptophane biosensor and xenonHuman Carbonic Anhydrase II complexed with Cryptophane biosensor and xenon

Structural highlights

3cyu is a 1 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 1.7Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

CAH2_HUMAN Defects in CA2 are the cause of osteopetrosis autosomal recessive type 3 (OPTB3) [MIM:259730; also known as osteopetrosis with renal tubular acidosis, carbonic anhydrase II deficiency syndrome, Guibaud-Vainsel syndrome or marble brain disease. Osteopetrosis is a rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. The disorder occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Autosomal recessive osteopetrosis is usually associated with normal or elevated amount of non-functional osteoclasts. OPTB3 is associated with renal tubular acidosis, cerebral calcification (marble brain disease) and in some cases with mental retardation.[1] [2] [3] [4] [5]

Function

CAH2_HUMAN Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide. Can hydrate cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye.[6] [7]

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

Cryptophanes represent an exciting class of xenon-encapsulating molecules that can be exploited as probes for nuclear magnetic resonance imaging. The 1.70 A resolution crystal structure of a cryptophane-derivatized benezenesulfonamide complexed with human carbonic anhydrase II shows how an encapsulated xenon atom can be directed to a specific biological target. The crystal structure confirms binding measurements indicating that the cryptophane cage does not strongly interact with the surface of the protein, which may enhance the sensitivity of 129Xe NMR spectroscopic measurements in solution.

Structure of a 129Xe-cryptophane biosensor complexed with human carbonic anhydrase II.,Aaron JA, Chambers JM, Jude KM, Di Costanzo L, Dmochowski IJ, Christianson DW J Am Chem Soc. 2008 Jun 4;130(22):6942-3. Epub 2008 May 8. PMID:18461940[8]

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

See Also

References

  1. ↑ Venta PJ, Welty RJ, Johnson TM, Sly WS, Tashian RE. Carbonic anhydrase II deficiency syndrome in a Belgian family is caused by a point mutation at an invariant histidine residue (107 His----Tyr): complete structure of the normal human CA II gene. Am J Hum Genet. 1991 Nov;49(5):1082-90. PMID:1928091
  2. ↑ Roth DE, Venta PJ, Tashian RE, Sly WS. Molecular basis of human carbonic anhydrase II deficiency. Proc Natl Acad Sci U S A. 1992 Mar 1;89(5):1804-8. PMID:1542674
  3. ↑ Soda H, Yukizane S, Yoshida I, Koga Y, Aramaki S, Kato H. A point mutation in exon 3 (His 107-->Tyr) in two unrelated Japanese patients with carbonic anhydrase II deficiency with central nervous system involvement. Hum Genet. 1996 Apr;97(4):435-7. PMID:8834238
  4. ↑ Hu PY, Lim EJ, Ciccolella J, Strisciuglio P, Sly WS. Seven novel mutations in carbonic anhydrase II deficiency syndrome identified by SSCP and direct sequencing analysis. Hum Mutat. 1997;9(5):383-7. PMID:9143915 doi:<383::AID-HUMU1>3.0.CO;2-5 10.1002/(SICI)1098-1004(1997)9:5<383::AID-HUMU1>3.0.CO;2-5
  5. ↑ Shah GN, Bonapace G, Hu PY, Strisciuglio P, Sly WS. Carbonic anhydrase II deficiency syndrome (osteopetrosis with renal tubular acidosis and brain calcification): novel mutations in CA2 identified by direct sequencing expand the opportunity for genotype-phenotype correlation. Hum Mutat. 2004 Sep;24(3):272. PMID:15300855 doi:10.1002/humu.9266
  6. ↑ Briganti F, Mangani S, Scozzafava A, Vernaglione G, Supuran CT. Carbonic anhydrase catalyzes cyanamide hydration to urea: is it mimicking the physiological reaction? J Biol Inorg Chem. 1999 Oct;4(5):528-36. PMID:10550681
  7. ↑ Kim CY, Whittington DA, Chang JS, Liao J, May JA, Christianson DW. Structural aspects of isozyme selectivity in the binding of inhibitors to carbonic anhydrases II and IV. J Med Chem. 2002 Feb 14;45(4):888-93. PMID:11831900
  8. ↑ Aaron JA, Chambers JM, Jude KM, Di Costanzo L, Dmochowski IJ, Christianson DW. Structure of a 129Xe-cryptophane biosensor complexed with human carbonic anhydrase II. J Am Chem Soc. 2008 Jun 4;130(22):6942-3. Epub 2008 May 8. PMID:18461940 doi:http://dx.doi.org/10.1021/ja802214x

3cyu, resolution 1.70Å

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