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 reaction between cis-diamminedichloroplatinum(II) (CDDP), cisplatin, a common anticancer drug, and bovine pancreatic ribonuclease (RNase A), induces extensive protein aggregation, leading to the formation of one dimer, one trimer and higher oligomers whose yields depend on cisplatin/protein ratio. Structural and functional properties of the purified platinated species, together with their spontaneous dissociation and thermally induced denaturation, have been characterized. Platinated species preserve a significant, although reduced, ribonuclease activity. The high resistance of the dimers against dissociation and the different thermal unfolding profiles suggest a quaternary structure different from those of the well-known swapped dimers of RNase A.
Platinated oligomers of bovine pancreatic ribonuclease: Structure and stability.,Picone D, Donnarumma F, Ferraro G, Russo Krauss I, Fagagnini A, Gotte G, Merlino A J Inorg Biochem. 2015 May;146:37-43. doi: 10.1016/j.jinorgbio.2015.02.011. Epub, 2015 Feb 26. PMID:25756333[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
- ↑ Picone D, Donnarumma F, Ferraro G, Russo Krauss I, Fagagnini A, Gotte G, Merlino A. Platinated oligomers of bovine pancreatic ribonuclease: Structure and stability. J Inorg Biochem. 2015 May;146:37-43. doi: 10.1016/j.jinorgbio.2015.02.011. Epub, 2015 Feb 26. PMID:25756333 doi:http://dx.doi.org/10.1016/j.jinorgbio.2015.02.011
