Ontology highlight
ABSTRACT:
SUBMITTER: Acharya KR
PROVIDER: S-EPMC42336 | biostudies-other | 1995 Mar
REPOSITORIES: biostudies-other
Proceedings of the National Academy of Sciences of the United States of America 19950301 7
The capacity of angiogenin (Ang) to induce blood vessel growth is critically dependent on its ribonucleolytic activity. Crystallography and mutagenesis of human Ang have previously shown that its pyrimidine binding site is obstructed by Gln-117, implying that a conformational change is a key part of the mechanism of Ang action. The 1.5-A-resolution crystal structure of bovine Ang, in which glutamic acid is substituted for Gln-117, now confirms that a blocked active site is characteristic of thes ...[more]