1E7H

HUMAN SERUM ALBUMIN COMPLEXED WITH HEXADECANOIC ACID (PALMITIC ACID)

Summary for 1E7H

• Entry DOI: 10.2210/pdb1e7h/pdb
• Related: 1AO6 1BJ5 1BKE 1BM0 1E78 1E7A 1E7B 1E7C 1E7E 1E7F 1E7G 1E7I 1UOR
• Descriptor: SERUM ALBUMIN, PALMITIC ACID (3 entities in total)
• Functional Keywords: plasma protein, metal-binding, lipid-binding
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 1
• Total formula weight: 68366.19

Authors

Bhattacharya, A.A.,Gruene, T.,Curry, S. (deposition date: 2000-08-29, release date: 2000-12-08, Last modification date: 2023-12-13)

Primary citation

Bhattacharya, A.A.,Grune, T.,Curry, S.
Crystallographic Analysis Reveals Common Modes of Binding of Medium and Long-Chain Fatty Acids to Human Serum Albumin
J.Mol.Biol., 303:721-, 2000

PubMed Abstract: Human serum albumin (HSA) is an abundant plasma protein that is responsible for the transport of fatty acids. HSA also binds and perturbs the pharmacokinetics of a wide range of drug compounds. Binding studies have revealed significant interactions between fatty acid and drug-binding sites on albumin but high-resolution structural information on ligand binding to the protein has been lacking. We report here a crystallographic study of five HSA-fatty acid complexes formed using saturated medium-chain and long-chain fatty acids (C10:0, C12:0, C14:0, C16:0 and C18:0). A total of seven binding sites that are occupied by all medium-chain and long-chain fatty acids have been identified, although medium-chain fatty acids are found to bind at additional sites on the protein, yielding a total of 11 distinct binding locations. Comparison of the different complexes reveals key similarities and significant differences in the modes of binding, and serves to rationalise much of the biochemical data on fatty acid interactions with albumin. The two principal drug-binding sites, in sub-domains IIA and IIIA, are observed to be occupied by fatty acids and one of them (in IIIA) appears to coincide with a high-affinity long-chain fatty acid binding site.

PubMed: 11061971
DOI: 10.1006/JMBI.2000.4158

Experimental method

X-RAY DIFFRACTION (2.43 Å)