View source for 6t42


==Bovine lactoglobulin complex with decanol==
<StructureSection load='6t42' size='340' side='right'caption='[[6t42]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6t42]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5eee 5eee]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T42 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T42 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]] 1.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DE1:DECAN-1-OL'>DE1</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=6t42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t42 OCA], [https://pdbe.org/6t42 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t42 RCSB], [https://www.ebi.ac.uk/pdbsum/6t42 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t42 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 ==
Ovine betaâlactoglobulin was characterized by spectroscopic (CD), calorimetric (ITC) and X-ray structural studies. The structure of ovine betaâlactoglobulin complex with decanol showed that tight packing of molecules in the crystalline phase enforces a distortion of protein flexible loops resulting in the formation of an asymmetric dimer. The loops surrounding beta-barrel in ovine lactoglobulin possessed the same conformational flexibility as observed previously in other lactoglobulins and the change of their conformation regulates the access to the binding pocket. The structure of asymmetric dimer revealed a new region in beta-barrel where ligand polar group can be located. These findings indicated protein adaptability to ligand dimensions and inter- and intramolecular interactions in the crystalline phase. Calorimetric and crystallographic studies provided the experimental evidence that ovine lactoglobulin is able to bind aliphatic ligands. Thermodynamic parameters of sodium dodecyl sulfate binding determined by ITC at pH 7.5 had Ka, DeltaH, TDeltaS and DeltaG values similar to those observed for bovine and caprine protein indicating the same mechanism of ligand binding.

Conformational flexibility and ligand binding properties of ovine beta-lactoglobulin.,Loch J, Bonarek P, Lewinski K Acta Biochim Pol. 2019 Dec 27;66(4):577-584. doi: 10.18388/abp.2019_2883. PMID:31880900<ref>PMID:31880900</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6t42" 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: Kopec M]]
[[Category: Lewinski K]]
[[Category: Loch JI]]