2bxp: Difference between revisions
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==Overview== | ==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. | 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. | ||
==Disease== | |||
Known diseases associated with this structure: Analbuminemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=103600 103600]], Dysalbuminemic hyperthyroxinemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=103600 103600]], Dysalbuminemic hyperzincemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=103600 103600]] | |||
==About this Structure== | ==About this Structure== | ||
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[[Category: transport protein]] | [[Category: transport protein]] | ||
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Revision as of 22:01, 12 November 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. 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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