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| | ==The crystal structure of the human carbonic anhydrase XIV== | | ==The crystal structure of the human carbonic anhydrase XIV== |
| - | <StructureSection load='4lu3' size='340' side='right' caption='[[4lu3]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='4lu3' size='340' side='right'caption='[[4lu3]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4lu3]] is a 1 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=4LU3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LU3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4lu3]] 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=4LU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LU3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AZM:5-ACETAMIDO-1,3,4-THIADIAZOLE-2-SULFONAMIDE'>AZM</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CA14, UNQ690/PRO1335 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4lu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lu3 OCA], [https://pdbe.org/4lu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lu3 RCSB], [https://www.ebi.ac.uk/pdbsum/4lu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lu3 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </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=4lu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lu3 OCA], [http://pdbe.org/4lu3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lu3 RCSB], [http://www.ebi.ac.uk/pdbsum/4lu3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lu3 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CAH14_HUMAN CAH14_HUMAN]] Reversible hydration of carbon dioxide. | + | [https://www.uniprot.org/uniprot/CAH14_HUMAN CAH14_HUMAN] Reversible hydration of carbon dioxide. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Carbonic anhydrase|Carbonic anhydrase]] | + | *[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Carbonate dehydratase]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]] | + | [[Category: Large Structures]] |
| - | [[Category: Alterio, V]] | + | [[Category: Alterio V]] |
| - | [[Category: Monti, S M]] | + | [[Category: De Simone G]] |
| - | [[Category: Simone, G De]]
| + | [[Category: Monti SM]] |
| - | [[Category: Glycoprotein]] | + | |
| - | [[Category: Lyase-lyase inhibitor complex]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Zinc binding]]
| + | |
| Structural highlights
4lu3 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.
| | Ligands: | , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
CAH14_HUMAN Reversible hydration of carbon dioxide.
Publication Abstract from PubMed
Carbonic anhydrase isoform XIV (CA XIV) is the last member of the human (h) CA family discovered so far, being localized in brain, kidneys, colon, small intestine, urinary bladder, liver, and spinal cord. It has recently been described as a possible drug target for treatment of epilepsy, some retinopathies as well as some skin tumors. Human carbonic anhydrase (hCA) XIV is a membrane-associated protein consisting of an N-terminal extracellular domain, a putative transmembrane region, and a small cytoplasmic tail. In this article, we report the expression, purification, and the crystallographic structure of the entire extracellular domain of this enzyme. The analysis of the structure revealed the typical alpha-CA fold, in which a 10-stranded beta-sheet forms the core of the molecule, while the comparison with all the other membrane associated isoforms (hCAs IV, IX, and XII) allowed to identify the diverse oligomeric arrangement and the sequence and structural differences observed in the region 127-136 as the main factors to consider in the design of selective inhibitors for each one of the membrane associated alpha-CAs. (c) 2013 Wiley Periodicals, Inc. Biopolymers 101: 769-778, 2014.
The structural comparison between membrane-associated human carbonic anhydrases provides insights into drug design of selective inhibitors.,Alterio V, Pan P, Parkkila S, Buonanno M, Supuran CT, Monti SM, De Simone G Biopolymers. 2014 Jul;101(7):769-78. doi: 10.1002/bip.22456. PMID:24374484[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Alterio V, Pan P, Parkkila S, Buonanno M, Supuran CT, Monti SM, De Simone G. The structural comparison between membrane-associated human carbonic anhydrases provides insights into drug design of selective inhibitors. Biopolymers. 2014 Jul;101(7):769-78. doi: 10.1002/bip.22456. PMID:24374484 doi:http://dx.doi.org/10.1002/bip.22456
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