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1ang

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1ang, resolution 2.40Å ()
Sites: and
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

Publication Abstract from PubMed

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.

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1ang is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Acharya KR, Shapiro R, Allen SC, Riordan JF, Vallee BL. Crystal structure of human angiogenin reveals the structural basis for its functional divergence from ribonuclease. Proc Natl Acad Sci U S A. 1994 Apr 12;91(8):2915-9. PMID:8159679
  • Kobe B, Deisenhofer J. Mechanism of ribonuclease inhibition by ribonuclease inhibitor protein based on the crystal structure of its complex with ribonuclease A. J Mol Biol. 1996 Dec 20;264(5):1028-43. PMID:9000628 doi:10.1006/jmbi.1996.0694

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