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2OCT

Stefin B (Cystatin B) tetramer

2OCT の概要
エントリーDOI10.2210/pdb2oct/pdb
分子名称Cystatin B (2 entities in total)
機能のキーワードstefin, cystatin, amyloid, domain-swapping, hand shaking, proline isomerization, protein binding
由来する生物種Homo sapiens (human)
細胞内の位置Cytoplasm: P04080
タンパク質・核酸の鎖数2
化学式量合計22327.07
構造登録者
Jenko Kokalj, S.,Guncar, G.,Turk, D. (登録日: 2006-12-21, 公開日: 2007-04-03, 最終更新日: 2023-08-30)
主引用文献Jenko Kokalj, S.,Guncar, G.,Stern, I.,Morgan, G.,Rabzelj, S.,Kenig, M.,Staniforth, R.A.,Waltho, J.P.,Zerovnik, E.,Turk, D.
Essential role of proline isomerization in stefin B tetramer formation.
J.Mol.Biol., 366:1569-1579, 2007
Cited by
PubMed Abstract: Here we present the tetrameric structure of stefin B, which is the result of a process by which two domain-swapped dimers of stefin B are transformed into tetramers. The transformation involves a previously unidentified process of extensive intermolecular contacts, termed hand shaking, which occurs concurrently with trans to cis isomerization of proline 74. This proline residue is widely conserved throughout the cystatin superfamily, a member of which, human cystatin C, is the key protein in cerebral amyloid angiopathy. These results are consistent with the hypothesis that isomerization of proline residues can play a decisive role in amyloidogenesis.
PubMed: 17217964
DOI: 10.1016/j.jmb.2006.12.025
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.4 Å)
構造検証レポート
Validation report summary of 2oct
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2026-04-08に公開中

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