1BJ5

HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACID

Summary for 1BJ5

• Entry DOI: 10.2210/pdb1bj5/pdb
• Descriptor: HUMAN SERUM ALBUMIN, MYRISTIC ACID (2 entities in total)
• Functional Keywords: plasma protein, metal-binding, lipid-binding
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P02768
• Total number of polymer chains: 1
• Total formula weight: 67713.07

Authors

Curry, S.,Mandelkow, H.,Brick, P.,Franks, N. (deposition date: 1998-07-02, release date: 1998-11-04, Last modification date: 2024-11-13)

Primary citation

Curry, S.,Mandelkow, H.,Brick, P.,Franks, N.
Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites.
Nat.Struct.Biol., 5:827-835, 1998

PubMed Abstract: 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.

PubMed: 9731778
DOI: 10.1038/1869

Experimental method

X-RAY DIFFRACTION (2.5 Å)