Ribonucleases

Ribonucleases

Structures and Functions
1997, Pages 305-341, III-VI
Ribonucleases

10 - Crystallographic Studies of Ribonuclease Complexes

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This chapter focuses on ribonuclease complexes and crystallographic studies of these complexes. Bovine pancreatic ribonuclease A hydrolyzes single-stranded RNA. Ribonuclease S (RNase S), an active variant of RNase A, can be produced by cleavage of the peptide bond between residues 20 and 21 by subtilisin. Early biochemical studies have shown that RNase A prefers a pyrimidine base on the 3′ side of the RNA cleavage site. Crystallographic studies of RNase A and RNase S with substrate analogs, a transition state analog, products, and inhibitors have been carried out to provide a structural basis of substrate specificity, catalysis, and inhibition to complement the biochemical and biophysical investigations of this enzyme. These studies provide details of how nucleotides and other ligands interact with the enzyme. This chapter discusses about phosphate/sulfate-free RNase, and explains concepts related to phosphate/sulfate-binding site. It also describes product–RNase complexes and nonproductive ligand–RNase complexes. An overview of transition state analog–RNase complex is presented in the chapter. The chapter elaborates in detail about substrate analog–RNase complexes, and concludes with a discussion on semisynthetic RNases.

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