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Article

Site-specific mutagenesis reveals differences in the structural bases for tight binding of RNase inhibitor to angiogenin and RNase A.

Proceedings of the National Academy of Sciences of the United States of America - 4 Mar 1997

Chen C Z, Shapiro R

Abstract excerpt

RNase inhibitor (RI) binds with extraordinary affinity (Ki approximately 10(-13)-10(-16) M) to diverse proteins in the pancreatic RNase superfamily. In the present study, the structural basis for the recognition of two RI ligands, human angiogenin (Ang) and bovine RNase A, has been investigated by site-specific mutagenesis of human RI and Ang. The RI residues examined were those that appear to form strong...

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Identifiers

PMID: 9050852
DOI: 10.1073/pnas.94.5.1761
PMCID: PMC19990

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Site-specific mutagenesis reveals differences in the structural bases for tight binding of RNase inhibitor to angiogenin and RNase A.PMID 9050852Read ↗

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