1qbn: Difference between revisions

Revision as of 14:19, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1qbn.png

Template:STRUCTURE 1qbn

BOVINE TRYPSIN 2-[AMINO(IMINO)METHYL]-2-HYDROXYPHENOXY]-6-[3-(4,5-DIHYDRO-1H-IMIDAZOL-2-YL)PHENOXY]PYRIDINE-4-CARBOXYLIC ACID (ZK-806688) COMPLEXBOVINE TRYPSIN 2-[AMINO(IMINO)METHYL]-2-HYDROXYPHENOXY]-6-[3-(4,5-DIHYDRO-1H-IMIDAZOL-2-YL)PHENOXY]PYRIDINE-4-CARBOXYLIC ACID (ZK-806688) COMPLEX

Template:ABSTRACT PUBMED 10417407

About this StructureAbout this Structure

1QBN is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Crystallographic analysis of potent and selective factor Xa inhibitors complexed to bovine trypsin., Whitlow M, Arnaiz DO, Buckman BO, Davey DD, Griedel B, Guilford WJ, Koovakkat SK, Liang A, Mohan R, Phillips GB, Seto M, Shaw KJ, Xu W, Zhao Z, Light DR, Morrissey MM, Acta Crystallogr D Biol Crystallogr. 1999 Aug;55(Pt 8):1395-404. PMID:10417407

Page seeded by OCA on Tue Jul 29 14:19:28 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1qbn.jpg|left|200px]]
+{{Seed}}
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 {{STRUCTURE_1qbn|  PDB=1qbn  |  SCENE=  }}
-'''BOVINE TRYPSIN 2-[AMINO(IMINO)METHYL]-2-HYDROXYPHENOXY]-6-[3-(4,5-DIHYDRO-1H-IMIDAZOL-2-YL)PHENOXY]PYRIDINE-4-CARBOXYLIC ACID (ZK-806688) COMPLEX'''
+===BOVINE TRYPSIN 2-[AMINO(IMINO)METHYL]-2-HYDROXYPHENOXY]-6-[3-(4,5-DIHYDRO-1H-IMIDAZOL-2-YL)PHENOXY]PYRIDINE-4-CARBOXYLIC ACID (ZK-806688) COMPLEX===
-==Overview==
+<!--
-Factor Xa is a serine protease which activates thrombin (factor IIa) and plays a key regulatory role in the blood-coagulation cascade. Factor Xa is, therefore, an important target for the design of anti-thrombotics. Both factor Xa and thrombin share sequence and structural homology with trypsin. As part of a factor Xa inhibitor-design program, a number of factor Xa inhibitors were crystallographically studied complexed to bovine trypsin. The structures of one diaryl benzimidazole, one diaryl carbazole and three diaryloxypyridines are described. All five compounds bind to trypsin in an extended conformation, with an amidinoaryl group in the S1 pocket and a second basic/hydrophobic moiety bound in the S4 pocket. These binding modes all bear a resemblance to the reported binding mode of DX-9065a in bovine trypsin and human factor Xa.
+The line below this paragraph, {{ABSTRACT_PUBMED_10417407}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10417407 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10417407}}
 ==About this Structure==
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 [[Category: S1 pocket]]
 [[Category: Serine proteinase]]
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