2bxf: Difference between revisions

Revision as of 21:11, 27 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:2bxf.png

Template:STRUCTURE 2bxf

HUMAN SERUM ALBUMIN COMPLEXED WITH DIAZEPAMHUMAN SERUM ALBUMIN COMPLEXED WITH DIAZEPAM

Template:ABSTRACT PUBMED 16169013

About this StructureAbout this Structure

2BXF 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

Page seeded by OCA on Sun Jul 27 21:11:54 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2bxf.gif|left|200px]]
+{{Seed}}
+[[Image:2bxf.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2bxf|  PDB=2bxf  |  SCENE=  }}
-'''HUMAN SERUM ALBUMIN COMPLEXED WITH DIAZEPAM'''
+===HUMAN SERUM ALBUMIN COMPLEXED WITH DIAZEPAM===
-==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
+(as it appears on PubMed at http://www.pubmed.gov), where 16169013 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16169013}}
 ==About this Structure==
@@ Line 34: / Line 38: @@
 [[Category: Metal-binding]]
 [[Category: Transport protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 20:55:59 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:11:54 2008''