Structural highlights
Function
THM1_THADA Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Russo Krauss I, Ferraro G, Merlino A. Cisplatin-Protein Interactions: Unexpected Drug Binding to N-Terminal Amine and Lysine Side Chains. Inorg Chem. 2016 Aug 15;55(16):7814-6. doi: 10.1021/acs.inorgchem.6b01234. Epub, 2016 Aug 2. PMID:27482735 doi:http://dx.doi.org/10.1021/acs.inorgchem.6b01234
