2lkk

Human L-FABP in complex with oleate

spinqualitylabelsall models 2lkk, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2lkk is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: OLA Related: 1lfo, 2ju3, 2ju7, 2f73, 2py1, 2l67, 2l68, 3stn, 3stk Gene: FABP1, FABPL (Homo sapiens) Resources: FirstGlance, OCA, RCSB, PDBsum Function [FABPL_HUMAN] Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport. Publication Abstract from PubMed 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 beta-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. Solution structure and backbone dynamics of human liver fatty acid binding protein: fatty acid binding revisited.,Cai J, Lucke C, Chen Z, Qiao Y, Klimtchuk E, Hamilton JA Biophys J. 2012 Jun 6;102(11):2585-94. doi: 10.1016/j.bpj.2012.04.039. Epub 2012 , Jun 5. PMID:22713574 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Fatty acid-binding protein

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