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1znc

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(New page: 200px<br /> <applet load="1znc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1znc, resolution 2.8&Aring;" /> '''HUMAN CARBONIC ANHYD...)
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[[Image:1znc.gif|left|200px]]<br />
 
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<applet load="1znc" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1znc, resolution 2.8&Aring;" />
 
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'''HUMAN CARBONIC ANHYDRASE IV'''<br />
 
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==Overview==
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==HUMAN CARBONIC ANHYDRASE IV==
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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, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?8942978 (full description)]]
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<StructureSection load='1znc' size='340' side='right'caption='[[1znc]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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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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</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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<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/initialview01.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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==About this Structure==
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==See Also==
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1ZNC is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with SO4 and ZN as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZNC OCA]].
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*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
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== References ==
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==Reference==
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<references/>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8942978 8942978]
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Christianson, D.W.]]
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[[Category: Christianson DW]]
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[[Category: Stams, T.]]
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[[Category: Stams T]]
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[[Category: SO4]]
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[[Category: ZN]]
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[[Category: gpi-anchor]]
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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://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 20:31:38 2007''
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Current revision

HUMAN CARBONIC ANHYDRASE IV

PDB ID 1znc

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