4GCC

Room temperature X-ray diffraction study of a 6-fold molar excess of a cisplatin/carboplatin mixture binding to HEWL, Dataset 1

Summary for 4GCC

• Entry DOI: 10.2210/pdb4gcc/pdb
• Related: 4DD0 4DD1 4DD2 4DD3 4DD4 4DD6 4DD7 4DD9 4DDA 4DDB 4DDC 4G49 4G4A 4G4B 4G4C 4G4H 4GCB 4GCD 4GCE 4GCF 4GCJ
• Descriptor: Lysozyme C, DIMETHYL SULFOXIDE, Cisplatin, ... (4 entities in total)
• Functional Keywords: cisplatin, carboplatin, histidine, relative toxicity, binding occupancy, x-ray radiation damage, radiation therapy, temperature variation and structure, hydrolase
• Biological source: Gallus gallus (chicken)
• Cellular location: Secreted: P00698
• Total number of polymer chains: 1
• Total formula weight: 15243.78

Authors

Helliwell, J.R.,Tanley, S.W.M. (deposition date: 2012-07-30, release date: 2013-01-02, Last modification date: 2024-10-16)

Primary citation

Helliwell, J.R.,Tanley, S.W.
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.
Acta Crystallogr.,Sect.D, 69:121-125, 2013

PubMed 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.

PubMed: 23275170
DOI: 10.1107/S090744491204423X

Experimental method

X-RAY DIFFRACTION (2 Å)