1ANG

CRYSTAL STRUCTURE OF HUMAN ANGIOGENIN REVEALS THE STRUCTURAL BASIS FOR ITS FUNCTIONAL DIVERGENCE FROM RIBONUCLEASE

Summary for 1ANG

• Entry DOI: 10.2210/pdb1ang/pdb
• Descriptor: ANGIOGENIN (1 entity in total)
• Functional Keywords: hydrolase (vascularization)
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P03950
• Total number of polymer chains: 1
• Total formula weight: 14169.04

Authors

Acharya, K.R.,Allen, S.,Shapiro, R.,Riordan, J.F.,Vallee, B.L. (deposition date: 1994-01-18, release date: 1995-04-20, Last modification date: 2024-10-09)

Primary citation

Acharya, K.R.,Shapiro, R.,Allen, S.C.,Riordan, J.F.,Vallee, B.L.
Crystal structure of human angiogenin reveals the structural basis for its functional divergence from ribonuclease.
Proc.Natl.Acad.Sci.USA, 91:2915-2919, 1994

PubMed 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.

PubMed: 8159679
DOI: 10.1073/pnas.91.8.2915

Experimental method

X-RAY DIFFRACTION (2.4 Å)