1znc

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{{Seed}}
 
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[[Image:1znc.png|left|200px]]
 
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==HUMAN CARBONIC ANHYDRASE IV==
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The line below this paragraph, containing "STRUCTURE_1znc", creates the "Structure Box" on the page.
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<StructureSection load='1znc' size='340' side='right'caption='[[1znc]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1znc]] 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=1ZNC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZNC FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1znc| PDB=1znc | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1znc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1znc OCA], [https://pdbe.org/1znc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1znc RCSB], [https://www.ebi.ac.uk/pdbsum/1znc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1znc ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/CAH4_HUMAN CAH4_HUMAN] Defects in CA4 are the cause of retinitis pigmentosa type 17 (RP17) [MIM:[https://omim.org/entry/600852 600852]. RP leads to degeneration of retinal photoreceptor cells. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. RP17 inheritance is autosomal dominant. Note=Defective acid overload removal from retina and retinal epithelium, due to mutant CA4, is responsible for photoreceptor degeneration, indicating that impaired pH homeostasis is the most likely cause underlying the RP17 phenotype.<ref>PMID:15563508</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/CAH4_HUMAN CAH4_HUMAN] Reversible hydration of carbon dioxide. May stimulate the sodium/bicarbonate transporter activity of SLC4A4 that acts in pH homeostasis. It is essential for acid overload removal from the retina and retina epithelium, and acid release in the choriocapillaris in the choroid.<ref>PMID:15563508</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zn/1znc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1znc ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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It has recently been demonstrated that the C-terminal deletion mutant of recombinant human carbonic anhydrase IV (G267X CA IV) converts the normally glycosylphosphatidylinositol-anchored enzyme into a soluble secretory form which has the same catalytic properties as the membrane-associated enzyme purified from human tissues. We have determined the three-dimensional structure of the secretory form of human CA IV by x-ray crystallographic methods to a resolution of 2.8 A. Although the zinc binding site and the hydrophobic substrate binding pocket of CA IV are generally similar to those of other mammalian isozymes, unique structural differences are found elsewhere in the active site. Two disufide linkages, Cys-6-Cys-11G and Cys-23-Cys-203, stabilize the conformation of the N-terminal domain. The latter disulfide additionally stabilizes an active site loop containing a cis-peptide linkage between Pro-201 and Thr-202 (this loop contains catalytic residue Thr-199). On the opposite side of the active site, the Val-131-Asp-136 segment adopts an extended loop conformation instead of an alpha-helix conformation as found in other isozymes. Finally, the C terminus is surrounded by a substantial electropositive surface potential, which is likely to stabilize the interaction of CA IV with the negatively charged phospholipid headgroups of the membrane. These structural features are unique to CA IV and provide a framework for the design of sulfonamide inhibitors selective for this particular isozyme.
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===HUMAN CARBONIC ANHYDRASE IV===
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Crystal structure of the secretory form of membrane-associated human carbonic anhydrase IV at 2.8-A resolution.,Stams T, Nair SK, Okuyama T, Waheed A, Sly WS, Christianson DW Proc Natl Acad Sci U S A. 1996 Nov 26;93(24):13589-94. PMID:8942978<ref>PMID:8942978</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1znc" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_8942978}}, adds the Publication Abstract to the page
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*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 8942978 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_8942978}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1ZNC is a 2 chains structure of sequences 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=1ZNC OCA].
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==Reference==
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<ref group="xtra">PMID:8942978</ref><references group="xtra"/>
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[[Category: Carbonate dehydratase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Christianson, D W.]]
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[[Category: Large Structures]]
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[[Category: Stams, T.]]
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[[Category: Christianson DW]]
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[[Category: Gpi-anchor]]
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[[Category: Stams T]]
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[[Category: Lyase]]
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[[Category: Membrane]]
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[[Category: Signal]]
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[[Category: Zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 23:37:13 2009''
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Current revision

HUMAN CARBONIC ANHYDRASE IV

PDB ID 1znc

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