1htd

From Proteopedia

(Difference between revisions)

Revision as of 02:58, 10 September 2015

STRUCTURAL INTERACTION OF NATURAL AND SYNTHETIC INHIBITORS WITH THE VENOM METALLOPROTEINASE, ATROLYSIN C (HT-D)

Structural highlights

1htd is a 2 chain structure with sequence from Crotalus atrox. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Activity:	Atrolysin C, with EC number 3.4.24.42
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[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).^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Baramova EN, Shannon JD, Bjarnason JB, Fox JW. Degradation of extracellular matrix proteins by hemorrhagic metalloproteinases. Arch Biochem Biophys. 1989 Nov 15;275(1):63-71. PMID:2817904
↑ Zhang D, Botos I, Gomis-Ruth FX, Doll R, Blood C, Njoroge FG, Fox JW, Bode W, Meyer EF. Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d). Proc Natl Acad Sci U S A. 1994 Aug 30;91(18):8447-51. PMID:8078901

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1htd"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Atrolysin_C Atrolysin C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.42 3.4.24.42] </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=1htd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1htd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1htd RCSB], [http://www.ebi.ac.uk/pdbsum/1htd PDBsum]</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=1htd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1htd OCA], [http://pdbe.org/1htd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1htd RCSB], [http://www.ebi.ac.uk/pdbsum/1htd PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HRTD_CROAT HRTD_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>
+[[http://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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1htd" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

1htd

From Proteopedia

Revision as of 02:58, 10 September 2015

STRUCTURAL INTERACTION OF NATURAL AND SYNTHETIC INHIBITORS WITH THE VENOM METALLOPROTEINASE, ATROLYSIN C (HT-D)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox