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- W200781673 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." @default.
- W200781673 created "2016-06-24" @default.
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- W200781673 date "2003-11-15" @default.
- W200781673 modified "2023-09-27" @default.
- W200781673 title "Crystallization and Crystal Structure Determination of Ribonuclease A-Ribonuclease Inhibitor Protein Complex" @default.
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- W200781673 doi "https://doi.org/10.1385/1-59259-233-3:201" @default.
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