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]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The total chemical synthesis of RNase A using modern chemical ligation methods is described, illustrating the significant advances that have been made in chemical protein synthesis since Gutte and Merrifield's pioneering preparation of RNase A in 1969. The identity of the synthetic product was confirmed through rigorous characterization, including the determination of the X-ray crystal structure to 1.1 Angstrom resolution.
Total synthesis by modern chemical ligation methods and high resolution (1.1 A) X-ray structure of ribonuclease A.,Boerema DJ, Tereshko VA, Kent SB Biopolymers. 2008;90(3):278-86. PMID:17610259[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
- ↑ Boerema DJ, Tereshko VA, Kent SB. Total synthesis by modern chemical ligation methods and high resolution (1.1 A) X-ray structure of ribonuclease A. Biopolymers. 2008;90(3):278-86. PMID:17610259 doi:10.1002/bip.20800
