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2n93
From Proteopedia
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| - | ''' | + | ==Solution structure of lcFABP== |
| + | <StructureSection load='2n93' size='340' side='right' caption='[[2n93]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2n93]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N93 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N93 FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2n93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n93 OCA], [http://pdbe.org/2n93 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n93 RCSB], [http://www.ebi.ac.uk/pdbsum/2n93 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:26373428</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2n93" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Lyu, P]] | [[Category: Lyu, P]] | ||
[[Category: Tseng, K]] | [[Category: Tseng, K]] | ||
| + | [[Category: Lipid binding protein]] | ||
Revision as of 16:58, 20 January 2016
Solution structure of lcFABP
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