6ge7: Difference between revisions

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-'''Unreleased structure'''
-The entry 6ge7 is ON HOLD
+==Thermodynamic, Crystallographic and Computational Studies of Non Mammalian Fatty Acid Binding to Bovine b-Lactoglobulin==
+<StructureSection load='6ge7' size='340' side='right' caption='[[6ge7]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6ge7]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GE7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GE7 FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EW8:nonadecanoic+acid'>EW8</scene></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=6ge7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ge7 OCA], [http://pdbe.org/6ge7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ge7 RCSB], [http://www.ebi.ac.uk/pdbsum/6ge7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ge7 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/LACB_BOVIN LACB_BOVIN]] Primary component of whey, it binds retinol and is probably involved in the transport of that molecule.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The milk protein beta-lactoglobulin has been widely studied since its discovery, both as a purified protein and in mixtures with other milk proteins, where its effect on the processing properties is of importance to the dairy industry. The protein can bind a variety of small hydrophobic molecules, which may allow its use as an oral delivery vehicle. In the present study we have examined the binding of odd-numbered fatty acids by isothermal calorimetry (ITC), X-ray crystallography and computer modelling to provide a clearer picture of the extent and variability of the central binding pocket. The Kd values for the fatty acids C13, C15, C16, C17 and C19 as determined by ITC are 1.93, 2.91, 3.05, 4.11 and 8.67x10(-7)M, respectively. The molecular structures revealed the ligands bound in the central cavity with generally well ordered lipophilic tails but significant positional variation at the carboxyl group end. In silico docking analyses identified the lipophilic interactions within the central cavity as the main driving force for binding with electrostatic interactions and H-bonds playing a minor role.
-Authors: Kontopidis, G., Rovoli, M.
+Thermodynamic, crystallographic and computational studies of non-mammalian fatty acid binding to bovine beta-Lactoglobulin.,Rovoli M, Thireou T, Choiset Y, Haertle T, Sawyer L, Eliopoulos E, Kontopidis G Int J Biol Macromol. 2018 Jun 4. pii: S0141-8130(18)30491-4. doi:, 10.1016/j.ijbiomac.2018.05.226. PMID:29879410<ref>PMID:29879410</ref>
-Description: Thermodynamic, Crystallographic and Computational Studies of Non Mammalian Fatty Acid Binding to Bovine b-Lactoglobulin
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6ge7" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Kontopidis, G]]
 [[Category: Rovoli, M]]
+[[Category: Fatty acid]]
+[[Category: Lactoglobulin]]
+[[Category: Non-mammalian]]
+[[Category: Transport protein]]