1atl
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1atl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Crotalus_atrox Crotalus atrox]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ATL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ATL FirstGlance]. <br> | <table><tr><td colspan='2'>[[1atl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Crotalus_atrox Crotalus atrox]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ATL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ATL FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0QI:O-METHYL-N-[(2S)-4-METHYL-2-(SULFANYLMETHYL)PENTANOYL]-L-TYROSINE'>0QI</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0QI:O-METHYL-N-[(2S)-4-METHYL-2-(SULFANYLMETHYL)PENTANOYL]-L-TYROSINE'>0QI</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1atl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1atl OCA], [https://pdbe.org/1atl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1atl RCSB], [https://www.ebi.ac.uk/pdbsum/1atl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1atl ProSAT]</span></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=1atl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1atl OCA], [https://pdbe.org/1atl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1atl RCSB], [https://www.ebi.ac.uk/pdbsum/1atl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1atl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/VM1AD_CROAT VM1AD_CROAT] Snake venom zinc metalloproteinase that causes hemorrhage by provoking the degradation of the sub-endothelial matrix proteins (fibronectin, laminin, type IV collagen, nidogen, and gelatins).<ref>PMID:2817904</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1atl ConSurf]. | </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=1atl ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The structure of the metalloproteinase and hemorrhagic toxin atrolysin C form d (EC 3.4.24.42), from the venom of the western diamondback rattlesnake Crotalus atrox, has been determined to atomic resolution by x-ray crystallographic methods. This study illuminates the nature of inhibitor binding with natural (< Glu-Asn-Trp, where < Glu is pyroglutamic acid) and synthetic (SCH 47890) ligands. The primary specificity pocket is exceptionally deep; the nature of inhibitor and productive substrate binding is discussed. Insights gained from the study of these complexes facilitate the design of potential drugs to treat diseases where matrix metalloproteinases have been implicated, e.g., arthritis and tumor metastasis. | ||
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| - | Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d).,Zhang D, Botos I, Gomis-Ruth FX, Doll R, Blood C, Njoroge FG, Fox JW, Bode W, Meyer EF Proc Natl Acad Sci U S A. 1994 Aug 30;91(18):8447-51. PMID:8078901<ref>PMID:8078901</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1atl" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Atrolysin C]] | ||
[[Category: Crotalus atrox]] | [[Category: Crotalus atrox]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Blood | + | [[Category: Blood C]] |
| - | [[Category: Bode | + | [[Category: Bode W]] |
| - | [[Category: Botos | + | [[Category: Botos I]] |
| - | [[Category: Doll | + | [[Category: Doll R]] |
| - | [[Category: Fox | + | [[Category: Fox JW]] |
| - | [[Category: Gomis-Rueth | + | [[Category: Gomis-Rueth F-X]] |
| - | [[Category: Meyer | + | [[Category: Meyer EF]] |
| - | [[Category: Njoroge | + | [[Category: Njoroge FG]] |
| - | [[Category: Zhang | + | [[Category: Zhang D]] |
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Revision as of 13:21, 13 March 2024
Structural interaction of natural and synthetic inhibitors with the VENOM METALLOPROTEINASE, ATROLYSIN C (FORM-D)
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Categories: Crotalus atrox | Large Structures | Blood C | Bode W | Botos I | Doll R | Fox JW | Gomis-Rueth F-X | Meyer EF | Njoroge FG | Zhang D
