This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1jd0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1jd0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jd0, resolution 1.50&Aring;" /> '''CRYSTAL STRUCTURE O...)
Current revision (07:51, 3 April 2024) (edit) (undo)
 
(19 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1jd0.gif|left|200px]]<br />
 
-
<applet load="1jd0" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1jd0, resolution 1.50&Aring;" />
 
-
'''CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF HUMAN CARBONIC ANHYDRASE XII COMPLEXED WITH ACETAZOLAMIDE'''<br />
 
-
==Overview==
+
==CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF HUMAN CARBONIC ANHYDRASE XII COMPLEXED WITH ACETAZOLAMIDE==
-
Overexpression of the zinc enzyme carbonic anhydrase (CA; EC ) XII is, observed in certain human cancers. This bitopic membrane protein contains, an N-terminal extracellular catalytic domain, a membrane-spanning, alpha-helix, and a small intracellular C-terminal domain. We have, determined the three-dimensional structure of the extracellular catalytic, domain of human CA XII by x-ray crystallographic methods at 1.55-A, resolution. The structure reveals a prototypical CA fold; however, two CA, XII domains associate to form an isologous dimer, an observation that is, confirmed by studies of the enzyme in solution. The identification of, signature GXXXG and GXXXS motifs in the transmembrane sequence that, facilitate helix-helix association is additionally consistent with dimeric, architecture. The dimer interface is situated so that the active site, clefts of each monomer are clearly exposed on one face of the dimer, and, the C termini are located together on the opposite face of the dimer to, facilitate membrane interaction. The amino acid composition of the, active-site cleft closely resembles that of the other CA isozymes in the, immediate vicinity of the catalytic zinc ion, but differs in the region of, the nearby alpha-helical "130's segment." The structure of the CA, XII-acetazolamide complex is also reported at 1.50-A resolution, and, prospects for the design of CA XII-specific inhibitors of possible, chemotherapeutic value are discussed.
+
<StructureSection load='1jd0' size='340' side='right'caption='[[1jd0]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1jd0]] 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=1JD0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JD0 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]] 1.5&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AZM:5-ACETAMIDO-1,3,4-THIADIAZOLE-2-SULFONAMIDE'>AZM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1jd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jd0 OCA], [https://pdbe.org/1jd0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jd0 RCSB], [https://www.ebi.ac.uk/pdbsum/1jd0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jd0 ProSAT]</span></td></tr>
 +
</table>
 +
== Disease ==
 +
[https://www.uniprot.org/uniprot/CAH12_HUMAN CAH12_HUMAN] Defects in CA12 are the cause of hyperchlorhidrosis isolated (HCHLH) [MIM:[https://omim.org/entry/143860 143860]. HCHLH is a disorder characterized by excessive sweating and increased sweat chloride levels. Affected individuals suffer from episodes of hyponatremic dehydration and report increased amounts of visible salt precipitates in sweat.<ref>PMID:21035102</ref>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/CAH12_HUMAN CAH12_HUMAN] Reversible hydration of carbon dioxide.
 +
== 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/jd/1jd0_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=1jd0 ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1JD0 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 ZN and AZM as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], 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=1JD0 OCA].
+
*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
Crystal structure of the dimeric extracellular domain of human carbonic anhydrase XII, a bitopic membrane protein overexpressed in certain cancer tumor cells., Whittington DA, Waheed A, Ulmasov B, Shah GN, Grubb JH, Sly WS, Christianson DW, Proc Natl Acad Sci U S A. 2001 Aug 14;98(17):9545-50. Epub 2001 Aug 7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11493685 11493685]
+
__TOC__
-
[[Category: Carbonate dehydratase]]
+
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Christianson, D.W.]]
+
[[Category: Christianson DW]]
-
[[Category: Grubb, J.H.]]
+
[[Category: Grubb JH]]
-
[[Category: Shah, G.N.]]
+
[[Category: Shah GN]]
-
[[Category: Sly, W.S.]]
+
[[Category: Sly WS]]
-
[[Category: Ulmasov, B.]]
+
[[Category: Ulmasov B]]
-
[[Category: Waheed, A.]]
+
[[Category: Waheed A]]
-
[[Category: Whittington, D.A.]]
+
[[Category: Whittington DA]]
-
[[Category: AZM]]
+
-
[[Category: ZN]]
+
-
[[Category: bitopic membrane protein]]
+
-
[[Category: extracellular domain]]
+
-
[[Category: human carbonic anhydrase xii]]
+
-
[[Category: type i membrane protein]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:39:39 2007''
+

Current revision

CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF HUMAN CARBONIC ANHYDRASE XII COMPLEXED WITH ACETAZOLAMIDE

PDB ID 1jd0

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools