6ryt: Difference between revisions
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<StructureSection load='6ryt' size='340' side='right'caption='[[6ryt]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='6ryt' size='340' side='right'caption='[[6ryt]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6ryt]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6ryt]] 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=6RYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RYT FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ryt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ryt OCA], [https://pdbe.org/6ryt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ryt RCSB], [https://www.ebi.ac.uk/pdbsum/6ryt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ryt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6ryt" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6ryt" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Beta-lactoglobulin 3D structures|Beta-lactoglobulin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bos taurus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kurpiewska | [[Category: Kurpiewska K]] | ||
[[Category: Lewinski | [[Category: Lewinski K]] | ||
[[Category: Loch | [[Category: Loch JI]] | ||
Latest revision as of 15:31, 24 January 2024
Engineered beta-lactoglobulin: variant M107LEngineered beta-lactoglobulin: variant M107L
Structural highlights
FunctionLACB_BOVIN Primary component of whey, it binds retinol and is probably involved in the transport of that molecule. Publication Abstract from PubMedRecombinant proteins play an important role in medicine and have diverse applications in industrial biotechnology. Lactoglobulin has shown great potential for use in targeted drug delivery and body fluid detoxification because of its ability to bind a variety of molecules. In order to modify the biophysical properties of beta-lactoglobulin, a series of single-site mutations were designed using a structure-based approach. A 3-dimensional structure alignment of homologous molecules led to the design of nine beta-lactoglobulin variants with mutations introduced in the binding pocket region. Seven stable and correctly folded variants (L39Y, I56F, L58F, V92F, V92Y, F105L, M107L) were thoroughly characterized by fluorescence, circular dichroism, isothermal titration calorimetry, size-exclusion chromatography, and X-ray structural investigations. The effects of the amino acid substitutions were observed as slight rearrangements of the binding pocket geometry, but they also significantly influenced the global properties of the protein. Most of the mutations increased the thermal/chemical stability without altering the dimerization constant or pH-dependent conformational behavior. The crystal structures reveal that the I56F and F105L mutations reduced the depth of the binding pocket, which is advantageous since it can reduce the affinity to endogenous fatty acids. The F105L mutant created a unique binding mode for a fatty acid, supporting the idea that lactoglobulin can be altered to bind unique molecules. Selected variants possessing a unique combination of their individual properties can be used for further, more advanced mutagenesis, and the presented results support further research using beta-lactoglobulin as a therapeutic delivery agent or a blood detoxifying molecule. Structure-based design approach to rational site-directed mutagenesis of beta-lactoglobulin.,Bonarek P, Loch JI, Tworzydlo M, Cooper DR, Milto K, Wrobel P, Kurpiewska K, Lewinski K J Struct Biol. 2020 Mar 10:107493. doi: 10.1016/j.jsb.2020.107493. PMID:32169624[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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