2bxp: Difference between revisions
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Revision as of 17:46, 30 October 2007
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HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE AND PHENYLBUTAZONE
OverviewOverview
Human serum albumin (HSA) is an abundant plasma protein that binds a, remarkably wide range of drugs, thereby restricting their free, active, concentrations. The problem of overcoming the binding affinity of lead, compounds for HSA represents a major challenge in drug development., Crystallographic analysis of 17 different complexes of HSA with a wide, variety of drugs and small-molecule toxins reveals the precise, architecture of the two primary drug-binding sites on the protein, identifying residues that are key determinants of binding specificity and, illuminating the capacity of both pockets for flexible accommodation., Numerous secondary binding sites for drugs distributed across the protein, have also been identified. The binding of fatty acids, the primary, physiological ligand for ... [(full description)]
About this StructureAbout this Structure
2BXP is a [Single protein] structure of sequence from [Homo sapiens] with MYR and P1Z as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Structural basis of the drug-binding specificity of human serum albumin., Ghuman J, Zunszain PA, Petitpas I, Bhattacharya AA, Otagiri M, Curry S, J Mol Biol. 2005 Oct 14;353(1):38-52. PMID:16169013
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