2bxk
From Proteopedia
(New page: 200px<br /> <applet load="2bxk" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bxk, resolution 2.40Å" /> '''HUMAN SERUM ALBUMIN...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2bxk.gif|left|200px]]<br /> | + | [[Image:2bxk.gif|left|200px]]<br /><applet load="2bxk" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2bxk" size=" | + | |
caption="2bxk, resolution 2.40Å" /> | caption="2bxk, resolution 2.40Å" /> | ||
'''HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE, AZAPROPAZONE AND INDOMETHACIN'''<br /> | '''HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE, AZAPROPAZONE AND INDOMETHACIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Human serum albumin (HSA) is an abundant plasma protein that binds a | + | 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== | ==Disease== | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2BXK 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, IMN and AZQ as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2BXK 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 <scene name='pdbligand=MYR:'>MYR</scene>, <scene name='pdbligand=IMN:'>IMN</scene> and <scene name='pdbligand=AZQ:'>AZQ</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BXK OCA]. |
==Reference== | ==Reference== | ||
| Line 17: | Line 16: | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bhattacharya, A | + | [[Category: Bhattacharya, A A.]] |
[[Category: Curry, S.]] | [[Category: Curry, S.]] | ||
[[Category: Ghuman, J.]] | [[Category: Ghuman, J.]] | ||
[[Category: Petitpas, I.]] | [[Category: Petitpas, I.]] | ||
| - | [[Category: Zunszain, P | + | [[Category: Zunszain, P A.]] |
[[Category: AZQ]] | [[Category: AZQ]] | ||
[[Category: IMN]] | [[Category: IMN]] | ||
| Line 35: | Line 34: | ||
[[Category: transport protein]] | [[Category: transport protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:42:39 2008'' |
Revision as of 14:42, 21 February 2008
|
HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE, AZAPROPAZONE AND INDOMETHACIN
Contents |
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.
Disease
Known diseases associated with this structure: Analbuminemia OMIM:[103600], Dysalbuminemic hyperthyroxinemia OMIM:[103600], Dysalbuminemic hyperzincemia OMIM:[103600]
About this Structure
2BXK is a Single protein structure of sequence from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.
Reference
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 Thu Feb 21 16:42:39 2008
Categories: Homo sapiens | Single protein | Bhattacharya, A A. | Curry, S. | Ghuman, J. | Petitpas, I. | Zunszain, P A. | AZQ | IMN | MYR | Albumin | Azapropazone | Carrier protein | Drug-binding | Indomethacin | Lipid-binding | Metal-binding | Myristate | Transport protein
