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. 1994 Apr 12;91(8):2915–2919. doi: 10.1073/pnas.91.8.2915

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

K R Acharya 1, R Shapiro 1, S C Allen 1, J F Riordan 1, B L Vallee 1
PMCID: PMC43485  PMID: 8159679

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 A, 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.

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Selected References

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