1gnj
From Proteopedia
HUMAN SERUM ALBUMIN COMPLEXED WITH CIS-5,8,11,14-EICOSATETRAENOIC ACID (ARACHIDONIC ACID)
Overview
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.
About this Structure
1GNJ is a Single protein structure of sequence from Homo sapiens. The following page contains interesting information on the relation of 1GNJ with [Serum Albumin]. Full crystallographic information is available from OCA.
Reference
Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids., Petitpas I, Grune T, Bhattacharya AA, Curry S, J Mol Biol. 2001 Dec 14;314(5):955-60. PMID:11743713 Page seeded by OCA on Fri May 2 17:47:14 2008
