1ANG

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

1ANG の概要

• エントリーDOI: 10.2210/pdb1ang/pdb
• 分子名称: ANGIOGENIN (1 entity in total)
• 機能のキーワード: hydrolase (vascularization)
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P03950
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14169.04

構造登録者

Acharya, K.R.,Allen, S.,Shapiro, R.,Riordan, J.F.,Vallee, B.L. (登録日: 1994-01-18, 公開日: 1995-04-20, 最終更新日: 2024-10-09)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.4 Å)