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3NZI

Substrate induced remodeling of the active site regulates HtrA1 activity

3NZI の概要
エントリーDOI10.2210/pdb3nzi/pdb
関連するPDBエントリー3NUM 3NWU
分子名称Serine protease HTRA1, Citrate synthase (2 entities in total)
機能のキーワードserine protease, degp, htra, protease, hydrolase-peptide inhibitor complex, hydrolase-hydrolase substrate complex, hydrolase/hydrolase substrate
由来する生物種Homo sapiens (human)
詳細
細胞内の位置Cell membrane : Q92743
タンパク質・核酸の鎖数2
化学式量合計37535.77
構造登録者
Truebestein, L.,Tennstaedt, A.,Hauske, P.,Krojer, T.,Kaiser, M.,Clausen, T.,Ehrmann, M. (登録日: 2010-07-16, 公開日: 2011-02-23, 最終更新日: 2024-11-20)
主引用文献Truebestein, L.,Tennstaedt, A.,Monig, T.,Krojer, T.,Canellas, F.,Kaiser, M.,Clausen, T.,Ehrmann, M.
Substrate-induced remodeling of the active site regulates human HTRA1 activity.
Nat.Struct.Mol.Biol., 18:386-388, 2011
Cited by
PubMed Abstract: Crystal structures of active and inactive conformations of the human serine protease HTRA1 reveal that substrate binding to the active site is sufficient to stimulate proteolytic activity. HTRA1 attaches to liposomes, digests misfolded proteins into defined fragments and undergoes substrate-mediated oligomer conversion. In contrast to those of other serine proteases, the PDZ domain of HTRA1 is dispensable for activation or lipid attachment, indicative of different underlying mechanistic features.
PubMed: 21297635
DOI: 10.1038/nsmb.2013
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.75 Å)
構造検証レポート
Validation report summary of 3nzi
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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