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| - | [[Image:1kuk.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1kuk| PDB=1kuk | SCENE= }} | | {{STRUCTURE_1kuk| PDB=1kuk | SCENE= }} |
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| - | '''Crystal Structure of a Taiwan Habu Venom Metalloproteinase complexed with pEKW.'''
| + | ===Crystal Structure of a Taiwan Habu Venom Metalloproteinase complexed with pEKW.=== |
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| - | ==Overview==
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| - | Venoms from crotalid and viperid snakes contain several peptide inhibitors which regulate the proteolytic activities of their snake-venom metalloproteinases (SVMPs) in a reversible manner under physiological conditions. In this report, we describe the high-resolution crystal structures of a SVMP, TM-3, from Taiwan habu (Trimeresurus mucrosquamatus) cocrystallized with the endogenous inhibitors pyroGlu-Asn-Trp (pENW), pyroGlu-Gln-Trp (pEQW) or pyroGlu-Lys-Trp (pEKW). The binding of inhibitors causes some of the residues around the inhibitor-binding environment of TM-3 to slightly move away from the active-site center, and displaces two metal-coordinated water molecules by the C-terminal carboxylic group of the inhibitors. This binding adopts a retro-manner principally stabilized by four possible hydrogen bonds. The Trp indole ring of the inhibitors is stacked against the imidazole of His143 in the S-1 site of the proteinase. Results from the study of synthetic inhibitor analogues showed the primary specificity of Trp residue of the inhibitors at the P-1 site, corroborating the stacking effect observed in our structures. Furthermore, we have made a detailed comparison of our structures with the binding modes of other inhibitors including batimastat, a hydroxamate inhibitor, and a barbiturate derivative. It suggests a close correlation between the inhibitory activity of an inhibitor and its ability to fill the S-1 pocket of the proteinase. Our work may provide insights into the rational design of small molecules that bind to this class of zinc-metalloproteinases.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12071970}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12071970 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12071970}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Alpha/beta protein]] | | [[Category: Alpha/beta protein]] |
| | [[Category: Retro-binding manner]] | | [[Category: Retro-binding manner]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:11:13 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:01:48 2008'' |
Revision as of 08:01, 2 July 2008
Template:STRUCTURE 1kuk
Crystal Structure of a Taiwan Habu Venom Metalloproteinase complexed with pEKW.
Template:ABSTRACT PUBMED 12071970
About this Structure
1KUK is a Single protein structure of sequence from Protobothrops mucrosquamatus. Full crystallographic information is available from OCA.
Reference
Determinants of the inhibition of a Taiwan habu venom metalloproteinase by its endogenous inhibitors revealed by X-ray crystallography and synthetic inhibitor analogues., Huang KF, Chiou SH, Ko TP, Wang AH, Eur J Biochem. 2002 Jun;269(12):3047-56. PMID:12071970
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