Structural highlights
Function
RNAS1_BOVIN Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA.[1]
Publication Abstract from PubMed
The crystal structure of the main adduct formed in the reaction between cisplatin and bovine pancreatic ribonuclease is reported here. Notably, in both of the protein molecules present in the asymmetric unit, platinum(II) binding takes place exclusively at the level of Met29. In one of the two molecules, the Gln28 side chain completes the platinum coordination sphere, anchoring the cisplatin fragment to the protein in a bidentate fashion. These results contain interesting implications for understanding the biological chemistry of this important drug.
Cisplatin binding to proteins: molecular structure of the ribonuclease a adduct.,Messori L, Merlino A Inorg Chem. 2014 Apr 21;53(8):3929-31. doi: 10.1021/ic500360f. Epub 2014 Apr 3. PMID:24694179[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ delCardayre SB, Ribo M, Yokel EM, Quirk DJ, Rutter WJ, Raines RT. Engineering ribonuclease A: production, purification and characterization of wild-type enzyme and mutants at Gln11. Protein Eng. 1995 Mar;8(3):261-73. PMID:7479688
- ↑ Messori L, Merlino A. Cisplatin binding to proteins: molecular structure of the ribonuclease a adduct. Inorg Chem. 2014 Apr 21;53(8):3929-31. doi: 10.1021/ic500360f. Epub 2014 Apr 3. PMID:24694179 doi:http://dx.doi.org/10.1021/ic500360f
