2i30
From Proteopedia
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Human serum albumin complexed with myristate and salicylic acid
Contents |
Overview
Human serum albumin (HSA) is the most abundant plasma protein in the human body with a plasma concentration of 0.6mM. HSA plays an important role in drug transport and metabolism. Enzymatic activity of HSA on different substrates or drugs has been studied and documented. The structural mechanism of this activity, however, is unknown. In this study, we have determined the crystal structures of HSA-myristate in a complex of aspirin and of salicylic acid, respectively. The crystal structure of HSA-myristate-aspirin illustrates that aspirin transfers acetyl group to Lys199 and is hydrolyzed into salicylic acid by HSA. The hydrolysis product, salicylic acid, remains bound to HSA at a similar location, but it shows a very different orientation when compared with the salicylic acid in the HSA-myristate-salicylic acid ternary complex. These results not only provide the structural evidence of esterase activity of HSA, and demonstrate the conformational plasticity of HSA on drug binding, but also may provide structural information for the modulation of HSA-drug interaction by computational approach based on HSA-drug structure.
Disease
Known diseases associated with this structure: Analbuminemia OMIM:[103600], Dysalbuminemic hyperthyroxinemia OMIM:[103600], Dysalbuminemic hyperzincemia OMIM:[103600]
About this Structure
2I30 is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Effect of human serum albumin on drug metabolism: structural evidence of esterase activity of human serum albumin., Yang F, Bian C, Zhu L, Zhao G, Huang Z, Huang M, J Struct Biol. 2007 Feb;157(2):348-55. Epub 2006 Sep 9. PMID:17067818
Page seeded by OCA on Thu Feb 21 17:48:31 2008
Categories: Homo sapiens | Single protein | Bian, C. | Huang, M. | Huang, Z. | Yang, F. | Zhao, G. | Zhu, L. | MYR | SAL | Lipid-binding | Metal-binding | Plasma protein
