Title: Crystallization and Crystal Structure Determination of Ribonuclease A-Ribonuclease Inhibitor Protein Complex
Abstract: Ribonuclease inhibitor (RI) is a cytoplasmic protein of ∼50 kDa that tightly binds and inhibits ribonucleases (RNases) from the pancreatic superfamily (). Diverse RNases with very limited sequence similarities, including RNase A, angiogenin, RNase-2 (also known as eosinophil-derived neurotoxin (EDN) or placental RNase), and RNase-4 are inhibited with K i values between 10−14 and 10−16 M. These affinities are among the highest reported for noncovalent binding of proteins. The binding occurs with 1∶1 stoichiometry. A subset of the pancreatic ribonuclease superfamily, including the amphibian ribonucleases such as frog-liver ribonuclease, sialic acid-binding lectin, and P-30 protein, are not inhibited by RI. The potent inhibitory activity of RI is believed to be utilized in RNA processing, angiogenesis, and protection of the cell from toxic ribonucleases.
Publication Year: 2003
Publication Date: 2003-11-14
Language: en
Type: review
Indexed In: ['crossref', 'pubmed']
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Cited By Count: 6
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