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==Energetic and structural effects of the Tanford transition on the ligand recognition of bovine Beta-lactoglobulin== | |||
<StructureSection load='7kp5' size='340' side='right'caption='[[7kp5]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KP5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KP5 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]] 2.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SDS:DODECYL+SULFATE'>SDS</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=7kp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kp5 OCA], [https://pdbe.org/7kp5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kp5 RCSB], [https://www.ebi.ac.uk/pdbsum/7kp5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kp5 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bovine beta-lactoglobulin, an abundant protein in whey, is a promising nanocarrier for peroral administration of drug-like hydrophobic molecules, a process that involves transit through the different acidic conditions of the human digestive tract. Among the several pH-induced conformational rearrangements that this lipocalin undergoes, the Tanford transition is particularly relevant. This transition, which occurs with a midpoint around neutral pH, involves a conformational change of the E-F loop that regulates accessibility to the primary binding site. The effect of this transition on the ligand binding properties of this protein has scarcely been explored. In this study, we carried out an energetic and structural characterization of beta-lactoglobulin molecular recognition at pH values above and below the zone in which the Tanford transition occurs. The combined analysis of crystallographic, calorimetric, and molecular dynamics data sheds new light on the interplay between self-association, ligand binding, and the Tanford pre- and post-transition conformational states, revealing novel aspects underlying the molecular recognition mechanism of this enigmatic lipocalin. | |||
Energetic and structural effects of the Tanford transition on ligand recognition of bovine beta-lactoglobulin.,Labra-Nunez A, Cofas-Vargas LF, Gutierrez-Magdaleno G, Gomez-Velasco H, Rodriguez-Hernandez A, Rodriguez-Romero A, Garcia-Hernandez E Arch Biochem Biophys. 2021 Jan 6;699:108750. doi: 10.1016/j.abb.2020.108750. PMID:33421379<ref>PMID:33421379</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7kp5" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Beta-lactoglobulin 3D structures|Beta-lactoglobulin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Rodriguez-Hernandez A]] | |||
[[Category: Rodriguez-Romero A]] | |||
Latest revision as of 11:55, 17 October 2024
Energetic and structural effects of the Tanford transition on the ligand recognition of bovine Beta-lactoglobulinEnergetic and structural effects of the Tanford transition on the ligand recognition of bovine Beta-lactoglobulin
Structural highlights
Publication Abstract from PubMedBovine beta-lactoglobulin, an abundant protein in whey, is a promising nanocarrier for peroral administration of drug-like hydrophobic molecules, a process that involves transit through the different acidic conditions of the human digestive tract. Among the several pH-induced conformational rearrangements that this lipocalin undergoes, the Tanford transition is particularly relevant. This transition, which occurs with a midpoint around neutral pH, involves a conformational change of the E-F loop that regulates accessibility to the primary binding site. The effect of this transition on the ligand binding properties of this protein has scarcely been explored. In this study, we carried out an energetic and structural characterization of beta-lactoglobulin molecular recognition at pH values above and below the zone in which the Tanford transition occurs. The combined analysis of crystallographic, calorimetric, and molecular dynamics data sheds new light on the interplay between self-association, ligand binding, and the Tanford pre- and post-transition conformational states, revealing novel aspects underlying the molecular recognition mechanism of this enigmatic lipocalin. Energetic and structural effects of the Tanford transition on ligand recognition of bovine beta-lactoglobulin.,Labra-Nunez A, Cofas-Vargas LF, Gutierrez-Magdaleno G, Gomez-Velasco H, Rodriguez-Hernandez A, Rodriguez-Romero A, Garcia-Hernandez E Arch Biochem Biophys. 2021 Jan 6;699:108750. doi: 10.1016/j.abb.2020.108750. PMID:33421379[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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