title: The crystal structure analysis of the relative binding of cisplatin and carboplatin in a mixture with histidine in a protein studied at 100 and 300 K with repeated X-ray irradiation.
abstract: The anticancer agents cisplatin and carboplatin bind to histidine in a protein. This crystal structure study at data-collection temperatures of 100 and 300 K examines their relative binding affinities to a histidine side chain and the effect of a high X-ray radiation dose of up to ∼1.8 MGy on the stability of the subsequent protein-Pt adducts. Cisplatin binding is visible at the histidine residue, but carboplatin binding is not. Five refined X-ray crystal structures are presented: one at 100 K as a reference and four at 300 K. The diffraction resolutions are 1.8, 2.0, 2.8, 2.9 and 3.5 Å.
authors.affiliation: School of Chemistry, University of Manchester, England, UK. john.helliwell@manchester.ac.uk
authors.forename: John R
authors.initials: JR
authors.lastname: Helliwell
authors.forename: Simon William Maurice
authors.initials: SW
authors.lastname: Tanley
mesh_terms: D000818:Animals; D016190:Carboplatin / Q000737:chemistry* / Q000378:metabolism; D002645:Chickens; D002945:Cisplatin / Q000737:chemistry* / Q000378:metabolism / Q000528:radiation effects; D003460:Crystallization; D018360:Crystallography, X-Ray; D006639:Histidine / Q000737:chemistry* / Q000378:metabolism / Q000528:radiation effects; D009113:Muramidase / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding / Q000528:radiation effects; D013696:Temperature; D014965:X-Rays / Q000009:adverse effects
chemical_list: D006639:Histidine; D016190:Carboplatin; C421864:hen egg lysozyme; D009113:Muramidase; D002945:Cisplatin