2n93

Solution structure of lcFABPSolution structure of lcFABP

Structural highlights 2n93 is a 1 chain structure with sequence from Abscondita cerata. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G1FKW0_9COLE Publication Abstract from PubMed Fatty acid-binding proteins (FABPs) are a family of proteins that modulate the transfer of various fatty acids in the cytosol and constitute a significant portion in many energy-consuming cells. The ligand binding properties and specific functions of a particular type of FABP seem to be diverse and depend on the respective binding cavity as well as the cell type from which this protein is derived. Previously, a novel FABP (lcFABP; lc: Luciola cerata) was identified in the light organ of Taiwanese fireflies. The lcFABP was proved to possess fatty acids binding capabilities, especially for fatty acids of length C14-C18. However, the structural details are unknown, and the structure-function relationship has remained to be further investigated. In this study, we finished the 1H, 15N and 13C chemical shift assignments of 15N/13C-enriched lcFABP by solution NMR spectroscopy. In addition, the secondary structure distribution was revealed based on the backbone N, H, Calpha, Halpha, C and side chain Cbeta assignments. These results can provide the basis for further structural exploration of lcFABP. H, N and C resonance assignments of light organ-associated fatty acid-binding protein of Taiwanese fireflies.,Tseng KL, Lee YZ, Chen YR, Lyu PC Biomol NMR Assign. 2015 Sep 15. PMID:26373428 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Fatty acid-binding protein 3D structures

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