2LKK

Human L-FABP in complex with oleate

Summary for 2LKK

• Entry DOI: 10.2210/pdb2lkk/pdb
• Related: 1LFO 2F73 2JU3 2JU7 2L67 2L68 2PY1 3STK 3STN
• NMR Information: BMRB: 17303
• Descriptor: Fatty acid-binding protein, liver, OLEIC ACID (2 entities in total)
• Functional Keywords: lipid binding protein, fatty acid carrier, holo form
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P07148
• Total number of polymer chains: 1
• Total formula weight: 14660.09

Authors

Cai, J.,Luecke, C.,Chen, Z.,Qiao, Y.,Klimtchuk, E.S.,Hamilton, J.A. (deposition date: 2011-10-13, release date: 2012-06-20, Last modification date: 2024-05-01)

Primary citation

Cai, J.,Lucke, C.,Chen, Z.,Qiao, Y.,Klimtchuk, E.,Hamilton, J.A.
Solution structure and backbone dynamics of human liver fatty acid binding protein: fatty acid binding revisited.
Biophys.J., 102:2585-2594, 2012

PubMed Abstract: Liver fatty acid binding protein (L-FABP), a cytosolic protein most abundant in liver, is associated with intracellular transport of fatty acids, nuclear signaling, and regulation of intracellular lipolysis. Among the members of the intracellular lipid binding protein family, L-FABP is of particular interest as it can i), bind two fatty acid molecules simultaneously and ii), accommodate a variety of bulkier physiological ligands such as bilirubin and fatty acyl CoA. To better understand the promiscuous binding and transport properties of L-FABP, we investigated structure and dynamics of human L-FABP with and without bound ligands by means of heteronuclear NMR. The overall conformation of human L-FABP shows the typical β-clam motif. Binding of two oleic acid (OA) molecules does not alter the protein conformation substantially, but perturbs the chemical shift of certain backbone and side-chain protons that are involved in OA binding according to the structure of the human L-FABP/OA complex. Comparison of the human apo and holo L-FABP structures revealed no evidence for an "open-cap" conformation or a "swivel-back" mechanism of the K90 side chain upon ligand binding, as proposed for rat L-FABP. Instead, we postulate that the lipid binding process in L-FABP is associated with backbone dynamics.

PubMed: 22713574
DOI: 10.1016/j.bpj.2012.04.039

Experimental method

SOLUTION NMR