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
A combination of mass spectrometry, Raman microspectroscopy, circular dichroism and X-ray crystallography has been used to obtain detailed information on the reaction of an iridium-based CO-releasing molecule (Ir-CORM), Cs2IrCl5CO, with a model protein, bovine pancreatic ribonuclease. The results show that Ir-compound fragments bind to the N-terminal amine and close to histidine and methionine side chains, and the CO ligand is retained for a long time. The data provide helpful information for identifying protein targets for Ir-CORMs and for studying the mechanism that allows them to exhibit their interesting biological properties.
Mapping the protein-binding sites for iridium(iii)-based CO-releasing molecules.,Caterino M, Petruk AA, Vergara A, Ferraro G, Marasco D, Doctorovich F, Estrin DA, Merlino A Dalton Trans. 2016 Jul 26;45(30):12206-12214. PMID:27411388[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
- ↑ Caterino M, Petruk AA, Vergara A, Ferraro G, Marasco D, Doctorovich F, Estrin DA, Merlino A. Mapping the protein-binding sites for iridium(iii)-based CO-releasing molecules. Dalton Trans. 2016 Jul 26;45(30):12206-12214. PMID:27411388 doi:http://dx.doi.org/10.1039/c6dt01685e
