View source for 5lkf


==Bovine beta-lactoglobulin complex with myristic acid at high pressure (0.55 GPa)==
<StructureSection load='5lkf' size='340' side='right'caption='[[5lkf]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5lkf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LKF FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></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=5lkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lkf OCA], [https://pdbe.org/5lkf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lkf RCSB], [https://www.ebi.ac.uk/pdbsum/5lkf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lkf ProSAT]</span></td></tr>
</table>
== Function ==
[https://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 ==
A number of studies were devoted to understanding an immunological effect of pressure-treated beta-lactoglobulin. In our previous work we have proved that high pressure significantly modifies beta-lactoglobulin conformation and consequently its physicochemical properties. Here, structure of beta-lactoglobulin complex with myristic acid determined at the highest accepted by the crystal pressure value of 550MPa is reported. Our results structurally prove that pressure noticeably modifies positions of the major beta-lactoglobulin epitopes. Considering the biological impact of observed changes in epitope regions, high pressure beta-lactoglobulin structure presents a step forward in understanding the pressure modification of food protein allergenicity. The conformational changes of pressurized beta-lactoglobulin did not support the hypothesis that proteolytic digestion facilitated by pressure is caused by an exposure of the digestive sites. Our findings demonstrate that high pressure protein crystallography can potentially identify the most pressure-sensitive fragments in allergens, and can therefore support development of hypoallergenic food products.

Towards understanding the effect of high pressure on food protein allergenicity: beta-lactoglobulin structural studies.,Kurpiewska K, Biela A, Loch JI, Lipowska J, Siuda M, Lewinski K Food Chem. 2019 Jan 1;270:315-321. doi: 10.1016/j.foodchem.2018.07.104. Epub 2018, Jul 17. PMID:30174052<ref>PMID:30174052</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5lkf" style="background-color:#fffaf0;"></div>

==See Also==
*[[Beta-lactoglobulin 3D structures|Beta-lactoglobulin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Garbacz K]]
[[Category: Kurpiewska K]]
[[Category: Lewinski K]]