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1fax

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{{STRUCTURE_1fax| PDB=1fax | SCENE= }}
{{STRUCTURE_1fax| PDB=1fax | SCENE= }}
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'''COAGULATION FACTOR XA INHIBITOR COMPLEX'''
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===COAGULATION FACTOR XA INHIBITOR COMPLEX===
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==Overview==
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The 3.0-A resolution x-ray structure of human des-Gla-coagulation factor Xa (fXa) has been determined in complex with the synthetic inhibitor DX-9065a. The binding geometry is characterized primarily by two interaction sites: the naphthamidine group is fixed in the S1 pocket by a typical salt bridge to Asp-189, while the pyrrolidine ring binds in the unique aryl-binding site (S4) of fXa. Unlike the large majority of inhibitor complexes with serine proteinases, Gly-216 (S3) does not contribute to hydrogen bond formation. In contrast to typical thrombin binding modes, the S2 site of fXa cannot be used by DX-9065a since it is blocked by Tyr-99, and the aryl-binding site (S4) of fXa is lined by carbonyl oxygen atoms that can accommodate positive charges. This has implications for natural substrate recognition as well as for drug design.
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(as it appears on PubMed at http://www.pubmed.gov), where 8939944 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8939944}}
==About this Structure==
==About this Structure==
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[[Category: Plasma]]
[[Category: Plasma]]
[[Category: Serine protease]]
[[Category: Serine protease]]
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Revision as of 23:58, 30 June 2008

Image:1fax.png

Template:STRUCTURE 1fax

COAGULATION FACTOR XA INHIBITOR COMPLEX

Template:ABSTRACT PUBMED 8939944

About this Structure

1FAX is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

X-ray structure of active site-inhibited clotting factor Xa. Implications for drug design and substrate recognition., Brandstetter H, Kuhne A, Bode W, Huber R, von der Saal W, Wirthensohn K, Engh RA, J Biol Chem. 1996 Nov 22;271(47):29988-92. PMID:8939944

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