1HMT

1.4 ANGSTROMS STRUCTURAL STUDIES ON HUMAN MUSCLE FATTY ACID BINDING PROTEIN: BINDING INTERACTIONS WITH THREE SATURATED AND UNSATURATED C18 FATTY ACIDS

Summary for 1HMT

• Entry DOI: 10.2210/pdb1hmt/pdb
• Descriptor: MUSCLE FATTY ACID BINDING PROTEIN, STEARIC ACID (3 entities in total)
• Functional Keywords: lipid-binding protein, lipid binding protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 15032.30

Authors

Young, A.C.M.,Scapin, G.,Kromminga, A.,Patel, S.B.,Veerkamp, J.H.,Sacchettini, J.C. (deposition date: 1994-01-02, release date: 1995-05-08, Last modification date: 2024-02-07)

Primary citation

Young, A.C.,Scapin, G.,Kromminga, A.,Patel, S.B.,Veerkamp, J.H.,Sacchettini, J.C.
Structural studies on human muscle fatty acid binding protein at 1.4 A resolution: binding interactions with three C18 fatty acids.
Structure, 2:523-534, 1994

PubMed Abstract: Muscle fatty acid binding protein (M-FABP) is one of a family of cytosolic lipid-binding proteins involved in fatty acid processing. In order to investigate the precise interactions between M-FABP and its ligands and to understand the structural basis of differential binding affinity, we have compared the structures of M-FABP in complex with three C18 fatty acids.

PubMed: 7922029
DOI: 10.1016/S0969-2126(00)00052-6

Experimental method

X-RAY DIFFRACTION (1.4 Å)