1bke

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spinqualitylabelsall models 1bke, resolution 3.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

HUMAN SERUM ALBUMIN IN A COMPLEX WITH MYRISTIC ACID AND TRI-IODOBENZOIC ACID

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

Human serum albumin (HSA) is the most abundant protein in the circulatory, system. Its principal function is to transport fatty acids, but it is also, capable of binding a great variety of metabolites and drugs. Despite, intensive efforts, the detailed structural basis of fatty acid binding to, HSA has remained elusive. We have now determined the crystal structure of, HSA complexed with five molecules of myristate at 2.5 A resolution. The, fatty acid molecules bind in long, hydrophobic pockets capped by polar, side chains, many of which are basic. These pockets are distributed, asymmetrically throughout the HSA molecule, despite its symmetrical, repeating domain structure.

Disease

Known diseases associated with this structure: Analbuminemia OMIM:[103600], Dysalbuminemic hyperthyroxinemia OMIM:[103600], Dysalbuminemic hyperzincemia OMIM:[103600]

About this Structure

1BKE is a Single protein structure of sequence from Homo sapiens with MYR and B3I as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites., Curry S, Mandelkow H, Brick P, Franks N, Nat Struct Biol. 1998 Sep;5(9):827-35. PMID:9731778

Page seeded by OCA on Mon Nov 12 16:11:03 2007