1ang
From Proteopedia
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'''CRYSTAL STRUCTURE OF HUMAN ANGIOGENIN REVEALS THE STRUCTURAL BASIS FOR ITS FUNCTIONAL DIVERGENCE FROM RIBONUCLEASE''' | '''CRYSTAL STRUCTURE OF HUMAN ANGIOGENIN REVEALS THE STRUCTURAL BASIS FOR ITS FUNCTIONAL DIVERGENCE FROM RIBONUCLEASE''' | ||
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[[Category: Shapiro, R.]] | [[Category: Shapiro, R.]] | ||
[[Category: Vallee, B L.]] | [[Category: Vallee, B L.]] | ||
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Revision as of 07:28, 2 May 2008
CRYSTAL STRUCTURE OF HUMAN ANGIOGENIN REVEALS THE STRUCTURAL BASIS FOR ITS FUNCTIONAL DIVERGENCE FROM RIBONUCLEASE
Overview
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.
About this Structure
1ANG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of human angiogenin reveals the structural basis for its functional divergence from ribonuclease., Acharya KR, Shapiro R, Allen SC, Riordan JF, Vallee BL, Proc Natl Acad Sci U S A. 1994 Apr 12;91(8):2915-9. PMID:8159679 Page seeded by OCA on Fri May 2 10:28:51 2008
