5nuj
From Proteopedia
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<StructureSection load='5nuj' size='340' side='right' caption='[[5nuj]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='5nuj' size='340' side='right' caption='[[5nuj]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5nuj]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NUJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NUJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5nuj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NUJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NUJ FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=Z80:3-(2-CHLORO-10H-PHENOTHIAZIN-10-YL)-N,N-DIMETHYLPROPAN-1-AMINE'>Z80</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=Z80:3-(2-CHLORO-10H-PHENOTHIAZIN-10-YL)-N,N-DIMETHYLPROPAN-1-AMINE'>Z80</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LGB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5nuj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nuj OCA], [http://pdbe.org/5nuj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nuj RCSB], [http://www.ebi.ac.uk/pdbsum/5nuj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nuj ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5nuj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nuj OCA], [http://pdbe.org/5nuj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nuj RCSB], [http://www.ebi.ac.uk/pdbsum/5nuj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nuj ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://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. | [[http://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 == | ||
| + | Chlorpromazine (CPZ) is a phenothiazine acting as dopamine antagonist. Aside from application in schizophrenia therapy, chlorpromazine is found to be a putative inhibitor of proteins involved in cancers, heritable autism disorder and prion diseases. Four new beta-lactoglobulin variants with double or triple substitutions: I56F/L39A, F105L/L39A, I56F/L39A/M107F or F105L/L39A/M107F changing the shape of the binding pocket were produced and their chlorpromazine binding properties have been investigated by X-ray crystallography, circular dichroism, isothermal titration calorimetry and thermophoresis. The CD spectra and crystal structures revealed that mutations do not affect the protein overall structure but in comparison to WT protein, variants possessing I56F substitution had lower stability while mutation F105L increased melting temperature of the protein. The new variants showed affinity to chlorpromazine in the range 4.2-15.4x10(3)M(-1). The CD spectra and crystal structures revealed complementarity of the binding pocket shape, to only one chlorpromazine chiral conformer. The (aR)-CPZ was bonded to variants containing I56F substitution while variants with F105L substitution preferred (aS)-CPZ. | ||
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| + | The engineered beta-lactoglobulin with complementarity to the chlorpromazine chiral conformers.,Loch JI, Bonarek P, Tworzydlo M, Lazinska I, Szydlowska J, Lipowska J, Rzesikowska K, Lewinski K Int J Biol Macromol. 2018 Mar 16;114:85-96. doi: 10.1016/j.ijbiomac.2018.03.074. PMID:29555509<ref>PMID:29555509</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5nuj" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bovin]] | ||
[[Category: Bonarek, P]] | [[Category: Bonarek, P]] | ||
[[Category: Lazinska, I]] | [[Category: Lazinska, I]] | ||
Revision as of 06:27, 18 April 2018
Engineered beta-lactoglobulin: variant I56F-L39A in complex with chlorpromazine (LG-FA-CLP)
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Categories: Bovin | Bonarek, P | Lazinska, I | Lewinski, K | Loch, J I | Szydlowska, J | Tworzydlo, M | Chlorpromazine | Complex | Lactoglobulin | Mutation | Transport protein
