1GNJ

HUMAN SERUM ALBUMIN COMPLEXED WITH cis-5,8,11,14-EICOSATETRAENOIC ACID (ARACHIDONIC ACID)

Summary for 1GNJ

• Entry DOI: 10.2210/pdb1gnj/pdb
• Related: 1AO6 1BJ5 1BKE 1BM0 1E78 1E7A 1E7B 1E7C 1E7E 1E7F 1E7G 1E7H 1E7I 1GNI 1H9Z 1HA2 1UOR
• Descriptor: SERUM ALBUMIN, ARACHIDONIC ACID (3 entities in total)
• Functional Keywords: plasma protein, metal-binding, lipid-binding, glycoprotein
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 1
• Total formula weight: 69006.96

Authors

Petitpas, I.,Gruene, T.,Bhattacharya, A.A.,Curry, S. (deposition date: 2001-10-05, release date: 2002-01-01, Last modification date: 2024-10-16)

Primary citation

Petitpas, I.,Gruene, T.,Bhattacharya, A.A.,Curry, S.
Crystal Structures of Human Serum Albumin Complexed with Monounsaturated and Polyunsaturated Fatty Acids.
J.Mol.Biol., 314:955-, 2001

PubMed Abstract: The primary ligands of human serum albumin (HSA), an abundant plasma protein, are non-esterified fatty acids. In vivo, the majority of fatty acids associated with the protein are unsaturated. We present here the first high-resolution crystal structures of HSA complexed with two important unsaturated fatty acids, the monounsaturated oleic acid (C18:1) and the polyunsaturated arachidonic acid (C20:4). Both compounds are observed to occupy the seven binding sites distributed across the protein that are also bound by medium and long-chain saturated fatty acids. Although C18:1 fatty acid binds each site on HSA in a conformation almost identical with that of the corresponding saturated compound (C18:0), the presence of multiple cis double bonds in C20:4 induces distinct binding configurations at some sites. The observed restriction on binding configurations plausibly accounts for differences in the pattern of binding affinities for the primary sites between polyunsaturated fatty acids and their saturated or monounsaturated counterparts.

PubMed: 11743713
DOI: 10.1006/JMBI.2000.5208

Experimental method

X-RAY DIFFRACTION (2.6 Å)