Open AccessA crystalline end product produced by the hydrolytic cleavage of an RNA-like fragment by an organometallointercalator: 1,10-phenanthroline-platlnum(II)-ethylenediamlne-cytidine 3′ monophoaphate
Author(s) -
Senadhi VijayKumar,
T. D. Sakore,
Henry M. Sobell
Publication year - 1984
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/12.8.3649
Subject(s) - cytidine , cleavage (geology) , stereochemistry , phenanthroline , biology , phosphodiester bond , rna , glycosidic bond , dna , hydrolysis , biochemistry , chemistry , enzyme , crystallography , paleontology , fracture (geology) , gene
1,10-Phenanthroline-platinum(II)-ethylenediamine ( PEPt ) forms a crystalline complex with cytidine-3'-phosphate (3'-CMP) and its structure has been determined by X-ray crystallography. 3'-CMP molecules are hemiprotonated and form hydrogen-bonded pairs that stack above and below the phenanthroline-platinum(II) drug molecule. Sugar residues are in the C2' endo conformation, with glycosidic torsional angles intermediate between the high and low anti forms. The structure is of particular interest since it forms as an end product of the hydrolytic cleavage of the dinucleoside monophosphate, CpG, by the platinum organometallointercalator ( PEPt ). This hydrolytic activity appears to be specific for the RNA dinucleoside monophosphate fragment, since deoxycytidylyl (3'-5')deoxyguanosine (d-CpG) and other deoxyribooligonucleotides are not cleaved under similar conditions.