View source for 7za0


==Mutant L58F of recombinant bovine beta-lactoglobulin in complex with pramocaine==
<StructureSection load='7za0' size='340' side='right'caption='[[7za0]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7za0]] 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=7ZA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZA0 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]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PX9:PRAMOCAINE'>PX9</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=7za0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7za0 OCA], [https://pdbe.org/7za0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7za0 RCSB], [https://www.ebi.ac.uk/pdbsum/7za0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7za0 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 ==
beta-Lactoglobulin (BLG) is a member of the lipocalin family. As other proteins from this group, BLG can be modified to bind specifically compounds of medical interests. The aim of this study was to evaluate the role of two mutations, L39Y and L58F, in the binding of topical anesthetic pramoxine (PRM) to beta-lactoglobulin. Circular dichroism spectroscopy, isothermal titration calorimetry (ITC), and X-ray crystallography were used to understand the mechanisms of BLG-PRM interactions. Studies were performed for three new BLG mutants: L39Y, L58F, and L39Y/L58F. ITC measurements indicated a significant increase in the affinity to the PRM of variants L58F and L39Y. Measurements taken for the double mutant L39Y/L58F showed the additivity of two mutations leading to about 80-fold increase in the affinity to PRM in comparison to natural protein BLG from bovine milk. The determined crystal structures revealed that pramoxine is accommodated in the beta-barrel interior of BLG mutants and stabilized by hydrophobic interactions. The observed additive effect of two mutations on drug binding opens the possibility for further designing of new BLG variants with high affinity to selected drugs.

beta-Lactoglobulin variants as potential carriers of pramoxine: Comprehensive structural and biophysical studies.,Bonarek P, Mularczyk D, Loch JI, Kurpiewska K, Dziedzicka-Wasylewska M J Mol Recognit. 2023 Oct;36(10):e3052. doi: 10.1002/jmr.3052. Epub 2023 Aug 23. PMID:37610054<ref>PMID:37610054</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7za0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Bonarek P]]
[[Category: Kurpiewska K]]
[[Category: Loch JI]]