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1dth

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Revision as of 16:37, 24 December 2014

METALLOPROTEASE

Structural highlights

1dth 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, RCSB, PDBsum

Function

[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).^[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

Matrix metalloproteinase enzymes have been implicated in degenerative processes like tumor cell invasion, metastasis, and arthritis. Specific metalloproteinase inhibitors have been used to block tumor cell proliferation. We have examined the interaction of batimastat (BB-94) with a metalloproteinase [atrolysin C (Ht-d), EC 3.4.24.42] active site at 2.0-angstroms resolution (R = 16.8%). The title structure exhibits an unexpected binding geometry, with the thiophene ring deeply inserted into the primary specificity site. This unprecedented binding geometry dramatizes the significance of the cavernous primary specificity site, pointing the way for the design of a new generation of potential antitumor drugs.

Batimastat, a potent matrix mealloproteinase inhibitor, exhibits an unexpected mode of binding.,Botos I, Scapozza L, Zhang D, Liotta LA, Meyer EF Proc Natl Acad Sci U S A. 1996 Apr 2;93(7):2749-54. PMID:8610113^[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
↑ Botos I, Scapozza L, Zhang D, Liotta LA, Meyer EF. Batimastat, a potent matrix mealloproteinase inhibitor, exhibits an unexpected mode of binding. Proc Natl Acad Sci U S A. 1996 Apr 2;93(7):2749-54. PMID:8610113

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/1dth"

@@ Line 7: / Line 7: @@
 <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=1dth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dth OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dth RCSB], [http://www.ebi.ac.uk/pdbsum/1dth 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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1dth

From Proteopedia

Revision as of 16:37, 24 December 2014

METALLOPROTEASE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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