View source for 7wql


==Bovin Beta-lactoglobulin binding with zinc ions==
<StructureSection load='7wql' size='340' side='right'caption='[[7wql]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7wql]] is a 2 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=7WQL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WQL 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]] 2.001&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7wql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wql OCA], [https://pdbe.org/7wql PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wql RCSB], [https://www.ebi.ac.uk/pdbsum/7wql PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wql 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 ==
Zinc plays a vital role in structural, catalysis, and signal regulation in the human body. Zinc deficiency leads to the dysfunction of many organs and immunity systems. Diet proteins have distinct effects on zinc uptake. However, the mechanisms are uncovered. Here we select three principal components from whey protein: alpha-lactalbumin, beta-lactoglobulin, and bovine serum albumin, which bind with zinc at different affinities, to evaluate the relationship between their potential zinc uptake and protein binding. The experimental data shows that beta-lactoglobulin could promote zinc uptake, alpha-lactalbumin has minor effects, whereas bovine serum albumin reduced zinc uptake in Caco-2 cell lines. Zinc binding effects on protein structure were thoroughly inspected through fluorescent spectroscopy and X-ray crystallography. Isothermal titration calorimetry revealed that three proteins have different binding affinities toward zinc ions. We speculate that protein binding eliminates toxic effects from free zinc, and the binding strength dominates zinc uptake.

Zinc binding strength of proteins dominants zinc uptake in Caco-2 cells.,Li T, Jiao R, Ma J, Zang J, Zhao G, Zhang T RSC Adv. 2022 Aug 1;12(33):21122-21128. doi: 10.1039/d2ra03565k. eCollection 2022 , Jul 21. PMID:35975046<ref>PMID:35975046</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7wql" style="background-color:#fffaf0;"></div>

==See Also==
*[[Alpha-lactalbumin 3D structures|Alpha-lactalbumin 3D structures]]
*[[Beta-lactoglobulin 3D structures|Beta-lactoglobulin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Li T]]
[[Category: Ma J]]
[[Category: Zang J]]
[[Category: Zhang T]]
[[Category: Zhao G]]