2Y0I

FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH TANKYRASE-2 (TNKS2) FRAGMENT PEPTIDE (21-MER)

2Y0I の概要

• エントリーDOI: 10.2210/pdb2y0i/pdb
• 関連するPDBエントリー: 1H2K 1H2L 1H2M 1H2N 1IZ3 1MZE 1MZF 1YCI 2CGN 2CGO 2W0X 2WA3 2WA4 2XUM
• 分子名称: HYPOXIA-INDUCIBLE FACTOR 1-ALPHA INHIBITOR, TANKYRASE-2, FE (II) ION, ... (7 entities in total)
• 機能のキーワード: oxidoreductase-peptide complex, dioxygenase, helix-loop-helix-beta, facial triad, asparaginyl/aspartyl hydroxylase, ankyrin repeat domain, oxidoreductase/peptide
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• 細胞内の位置: Nucleus: Q9NWT6; Cytoplasm: Q9H2K2
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 43611.50

構造登録者

Chowdhury, R.,McDonough, M.A.,Schofield, C.J. (登録日: 2010-12-02, 公開日: 2011-02-02, 最終更新日: 2023-12-20)

主引用文献

Yang, M.,Chowdhury, R.,Ge, W.,Hamed, R.B.,McDonough, M.A.,Claridge, T.D.,Kessler, B.M.,Cockman, M.E.,Ratcliffe, P.J.,Schofield, C.J.
Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains.
FEBS J., 278:1086-1097, 2011

PubMed Abstract: Factor-inhibiting hypoxia-inducible factor (FIH) is an Fe(II)/2-oxoglutarate-dependent dioxygenase that acts as a negative regulator of the hypoxia-inducible factor (HIF) by catalysing β-hydroxylation of an asparaginyl residue in its C-terminal transcriptional activation domain (CAD). In addition to the hypoxia-inducible factor C-terminal transcriptional activation domain (HIF-CAD), FIH also catalyses asparaginyl hydroxylation of many ankyrin repeat domain-containing proteins, revealing a broad sequence selectivity. However, there are few reports on the selectivity of FIH for the hydroxylation of specific residues. Here, we report that histidinyl residues within the ankyrin repeat domain of tankyrase-2 can be hydroxylated by FIH. NMR and crystallographic analyses show that the histidinyl hydroxylation occurs at the β-position. The results further expand the scope of FIH-catalysed hydroxylations.

PubMed: 21251231
DOI: 10.1111/j.1742-4658.2011.08022.x

実験手法

X-RAY DIFFRACTION (2.28 Å)