5l4r
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==X-ray structure of the adduct between thaumatin and cisplatin== | |
| + | <StructureSection load='5l4r' size='340' side='right' caption='[[5l4r]], [[Resolution|resolution]] 1.45Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5l4r]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L4R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5L4R FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=73M:BIS(AZANYL)-CHLORANYL-OXIDANYL-PLATINUM'>73M</scene>, <scene name='pdbligand=CPT:CISPLATIN'>CPT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></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=5l4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l4r OCA], [http://pdbe.org/5l4r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l4r RCSB], [http://www.ebi.ac.uk/pdbsum/5l4r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l4r ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/THM1_THADA THM1_THADA]] Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Literature studies carried out by mass spectrometry and X-ray crystallography have demonstrated that cisplatin is able to bind proteins mainly close to Met, His, and free Cys side chains. To identify possible alternative modes of cisplatin binding to proteins at the molecular level, here we have solved the high-resolution X-ray structure of the adduct formed in the reaction between the drug and the model protein thaumatin, which does not contain any His and free Cys residues and possesses just one buried Met. Our data reveal unexpected cisplatin binding sites on the protein surface that could have general significance: cisplatin fragments -[Pt(NH3)2Cl](+), -[Pt(NH3)Cl2], and -[Pt(NH3)2(OH2)](2+) bind to a protein N-terminus and close to Lys and Glu side chains. | ||
| - | + | Cisplatin-Protein Interactions: Unexpected Drug Binding to N-Terminal Amine and Lysine Side Chains.,Russo Krauss I, Ferraro G, Merlino A Inorg Chem. 2016 Aug 15;55(16):7814-6. doi: 10.1021/acs.inorgchem.6b01234. Epub, 2016 Aug 2. PMID:27482735<ref>PMID:27482735</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 5l4r" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Ferraro, G]] | [[Category: Ferraro, G]] | ||
| + | [[Category: Krauss, I Russo]] | ||
[[Category: Merlino, A]] | [[Category: Merlino, A]] | ||
| - | [[Category: | + | [[Category: Cisplatin]] |
| + | [[Category: Drug]] | ||
| + | [[Category: Model protein]] | ||
| + | [[Category: Plant protein]] | ||
Revision as of 19:30, 9 December 2016
X-ray structure of the adduct between thaumatin and cisplatin
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