Crystal structure of human angiogenin reveals the structural basis for its functional divergence from ribonuclease

K. Ravi Acharya, Robert Shapiro, Simon C. Allen, James F. Riordan, Bert L. Vallee

Research output: Contribution to journalArticlepeer-review

Abstract

Angiogenin, a potent inducer of neovascularization, is the only angiogenic molecule known to exhibit ribonucleolytic activity. Its overall structure, as determined at 2.4 Å, is similar to that of pancreatic ribonuclease A, but it differs markedly in several distinct areas, particularly the ribonucleolytic active center and the putative receptor binding site, both of which are critically involved in biological function. Most strikingly, the site that is spatially analogous to that for pyrimidine binding in ribonuclease A differs significantly in conformation and is 'obstructed' by glutamine-117. Movement of this and adjacent residues may be required for substrate binding to angiogenin and, hence, constitute a key part of its mechanism of action.

Original languageEnglish
Pages (from-to)2915-2919
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume91
Issue number8
DOIs
Publication statusPublished - 12 Apr 1994

ASJC Scopus subject areas

  • General

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