7bf8: Difference between revisions

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<StructureSection load='7bf8' size='340' side='right'caption='[[7bf8]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='7bf8' size='340' side='right'caption='[[7bf8]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7bf8]] 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=7BF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BF8 FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BF8 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]] 1.8&#8491;</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TE4:TETRACAINE'>TE4</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TE4:TETRACAINE'>TE4</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=7bf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bf8 OCA], [https://pdbe.org/7bf8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bf8 RCSB], [https://www.ebi.ac.uk/pdbsum/7bf8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bf8 ProSAT]</span></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=7bf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bf8 OCA], [https://pdbe.org/7bf8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bf8 RCSB], [https://www.ebi.ac.uk/pdbsum/7bf8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bf8 ProSAT]</span></td></tr>
</table>
</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) like other lipocalins can be modified by mutagenesis to re-direct its ligand binding properties. Local site-directed mutagenesis was used to change the geometry of the BLG ligand binding pocket and therefore change BLG ligand preferences. The presented studies are focused on previously described mutants L39Y, I56F, L58F, F105L, and M107L and two new BLG variants, L39K and F105A, and their interactions with local anesthetic drug tetracaine. Binding of tetracaine to BLG mutants was investigated by X-ray crystallography. Structural analysis revealed that for tetracaine binding, the shape of the binding pocket seems to be a more important factor than the substitutions influencing the number of interactions. Analyzed BLG mutants can be classified according to their binding properties to variants: capable of binding tetracaine in the beta-barrel (L58F, M107L); capable of accommodating tetracaine on the protein surface (I56F) and unable to bind tetracaine (F105L). Variants L39K, L39Y, and F105A, had a binding pocket blocked by endogenous fatty acids. The new tetracaine binding site was found in the I56F variant. The site localized on the surface near Arg124 and Trp19 was previously predicted by in silico studies and was confirmed in the crystal structure.
Interactions of new lactoglobulin variants with tetracaine: crystallographic studies of ligand binding to lactoglobulin mutants possessing single substitution in the binding pocket.,Loch J, Bonarek P, Siuda M, Wrobel P, Lewinski K Acta Biochim Pol. 2021 Mar 15;68(1):23-28. doi: 10.18388/abp.2020_5593. PMID:33719368<ref>PMID:33719368</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7bf8" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Beta-lactoglobulin 3D structures|Beta-lactoglobulin 3D structures]]
*[[Beta-lactoglobulin 3D structures|Beta-lactoglobulin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kaczor K]]
[[Category: Kaczor K]]
[[Category: Lewinski K]]
[[Category: Lewinski K]]
[[Category: Loch JI]]
[[Category: Loch JI]]

Latest revision as of 16:27, 6 November 2024

Mutant I56F of recombinant bovine beta-lactoglobulin in complex with tetracaineMutant I56F of recombinant bovine beta-lactoglobulin in complex with tetracaine

Structural highlights

Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

See Also

7bf8, resolution 1.80Å

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