2bxp: Difference between revisions

Revision as of 17:50, 28 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:2bxp.png

Template:STRUCTURE 2bxp

HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE AND PHENYLBUTAZONEHUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE AND PHENYLBUTAZONE

Template:ABSTRACT PUBMED 16169013

About this StructureAbout this Structure

2BXP is a Single protein structure of sequence from Homo sapiens. 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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE AND PHENYLBUTAZONE'''
+===HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE AND PHENYLBUTAZONE===
-==Overview==
+<!--
-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 the protein, is shown to alter the polarity and increase the volume of drug site 1. These results clarify the interpretation of accumulated drug binding data and provide a valuable template for design efforts to modulate the interaction with HSA.
+The line below this paragraph, {{ABSTRACT_PUBMED_16169013}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_16169013}}
 ==About this Structure==
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 [[Category: Albumin,carrier protein,lipid-binding,phenylbutazone]]
 [[Category: Metal-binding,drug-binding,myristate,transport protein]]
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