2n93: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 2n93 is ON HOLD  until Paper Publication
+==Solution structure of lcFABP==
+<StructureSection load='2n93' size='340' side='right'caption='[[2n93]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2n93]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Abscondita_cerata Abscondita cerata]. 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 [https://proteopedia.org/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'>[https://proteopedia.org/fgij/fg.htm?mol=2n93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n93 OCA], [https://pdbe.org/2n93 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n93 RCSB], [https://www.ebi.ac.uk/pdbsum/2n93 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n93 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/G1FKW0_9COLE G1FKW0_9COLE]
+<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.
-Authors: Tseng, K., Lyu, P.
+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>
-Description: Solution structure of lcFABP
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Lyu, P]]
+<div class="pdbe-citations 2n93" style="background-color:#fffaf0;"></div>
-[[Category: Tseng, K]]
+==See Also==
+*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Abscondita cerata]]
+[[Category: Large Structures]]
+[[Category: Lyu P]]
+[[Category: Tseng K]]