6ghh
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Thermodynamic, Crystallographic and Computational Studies of Non Mammalian Fatty Acid Binding to Bovine b-Lactoglobulin== | |
| + | <StructureSection load='6ghh' size='340' side='right' caption='[[6ghh]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6ghh]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GHH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GHH FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TDA:N-TRIDECANOIC+ACID'>TDA</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=6ghh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ghh OCA], [http://pdbe.org/6ghh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ghh RCSB], [http://www.ebi.ac.uk/pdbsum/6ghh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ghh 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 6ghh" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Kontopidis, G]] | [[Category: Kontopidis, G]] | ||
[[Category: Rovoli, M]] | [[Category: Rovoli, M]] | ||
| + | [[Category: Fatty acid]] | ||
| + | [[Category: Lactoglobulin]] | ||
| + | [[Category: Non-mammalian]] | ||
| + | [[Category: Transport protein]] | ||
Revision as of 05:56, 20 June 2018
Thermodynamic, Crystallographic and Computational Studies of Non Mammalian Fatty Acid Binding to Bovine b-Lactoglobulin
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