2bxp: Difference between revisions
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[[Image:2bxp.gif|left|200px]]<br /> | [[Image:2bxp.gif|left|200px]]<br /><applet load="2bxp" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="2bxp" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="2bxp, resolution 2.30Å" /> | caption="2bxp, resolution 2.30Å" /> | ||
'''HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE AND PHENYLBUTAZONE'''<br /> | '''HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE AND PHENYLBUTAZONE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2BXP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MYR and P1Z as [http://en.wikipedia.org/wiki/ligands ligands]. | 2BXP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MYR and P1Z as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:P1z Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BXP OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: transport protein]] | [[Category: transport protein]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 19:02:15 2007'' | ||
Revision as of 19:52, 18 December 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 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.
DiseaseDisease
Known diseases associated with this structure: Analbuminemia OMIM:[103600], Dysalbuminemic hyperthyroxinemia OMIM:[103600], Dysalbuminemic hyperzincemia OMIM:[103600]
About this StructureAbout this Structure
2BXP is a Single protein structure of sequence from Homo sapiens with MYR and P1Z as ligands. Known structural/functional Site: . 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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