6gfs: Difference between revisions
New page: '''Unreleased structure''' The entry 6gfs is ON HOLD Authors: Kontopidis, G., Rovoli, M. Description: Thermodynamic, Crystallographic and Computational Studies of Non Mammalian Fatty A... |
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The | ==Thermodynamic, Crystallographic and Computational Studies of Non Mammalian Fatty Acid Binding to Bovine b-Lactoglobulin== | ||
<StructureSection load='6gfs' size='340' side='right' caption='[[6gfs]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6gfs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GFS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GFS FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=F15:PENTADECANOIC+ACID'>F15</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LGB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</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=6gfs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gfs OCA], [http://pdbe.org/6gfs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gfs RCSB], [http://www.ebi.ac.uk/pdbsum/6gfs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gfs 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> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6gfs" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bovin]] | |||
[[Category: Kontopidis, G]] | [[Category: Kontopidis, G]] | ||
[[Category: Rovoli, M]] | [[Category: Rovoli, M]] | ||
[[Category: Fatty acid]] | |||
[[Category: Lactoglobulin]] | |||
[[Category: Non-mammalian]] | |||
[[Category: Transport protein]] | |||
Latest revision as of 09:19, 11 July 2018
Thermodynamic, Crystallographic and Computational Studies of Non Mammalian Fatty Acid Binding to Bovine b-LactoglobulinThermodynamic, Crystallographic and Computational Studies of Non Mammalian Fatty Acid Binding to Bovine b-Lactoglobulin
Structural highlights
Function[LACB_BOVIN] Primary component of whey, it binds retinol and is probably involved in the transport of that molecule. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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