2OCT
Stefin B (Cystatin B) tetramer
2OCT の概要
| エントリーDOI | 10.2210/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 | |
| 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: 17217964DOI: 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) |
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