1ha2
From Proteopedia
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HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACID AND THE S-(-) ENANTIOMER OF WARFARIN
Overview
Human serum albumin (HSA) is an abundant transport protein found in plasma, that binds a wide variety of drugs in two primary binding sites (I and II), and can have a significant impact on their pharmacokinetics. We have, determined the crystal structures at 2.5 A-resolution of HSA-myristate, complexed with the R-(+) and S-(-) enantiomers of warfarin, a widely used, anticoagulant that binds to the protein with high affinity. The structures, confirm that warfarin binds to drug site I (in subdomain IIA) in the, presence of fatty acids and reveal the molecular details of the, protein-drug interaction. The two enantiomers of warfarin adopt very, similar conformations when bound to the protein and make many of the same, specific contacts with amino acid side chains at the binding site, thus, ... [(full description)]
About this Structure
1HA2 is a [Single protein] structure of sequence from [Homo sapiens] with MYR and WRS as [ligands]. Full crystallographic information is available from [OCA].
Reference
Crystal structure analysis of warfarin binding to human serum albumin: anatomy of drug site I., Petitpas I, Bhattacharya AA, Twine S, East M, Curry S, J Biol Chem. 2001 Jun 22;276(25):22804-9. Epub 2001 Apr 2. PMID:11285262
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