3L1E
Bovine AlphaA crystallin Zinc Bound
3L1E の概要
| エントリーDOI | 10.2210/pdb3l1e/pdb |
| 関連するPDBエントリー | 3L1F 3L1G |
| 分子名称 | Alpha-crystallin A chain, ZINC ION, GLYCEROL, ... (4 entities in total) |
| 機能のキーワード | lens transparency, polydispersity, protein aggregation, crystallin, eye lens protein, chaperone |
| 由来する生物種 | Bos taurus (bovine) |
| 細胞内の位置 | Cytoplasm : P02470 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 12073.70 |
| 構造登録者 | Laganowsky, A.,Sawaya, M.R.,Cascio, D.,Eisenberg, D. (登録日: 2009-12-11, 公開日: 2010-05-12, 最終更新日: 2024-02-21) |
| 主引用文献 | Laganowsky, A.,Benesch, J.L.,Landau, M.,Ding, L.,Sawaya, M.R.,Cascio, D.,Huang, Q.,Robinson, C.V.,Horwitz, J.,Eisenberg, D. Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function. Protein Sci., 19:1031-1043, 2010 Cited by PubMed Abstract: Small heat shock proteins alphaA and alphaB crystallin form highly polydisperse oligomers that frustrate protein aggregation, crystallization, and amyloid formation. Here, we present the crystal structures of truncated forms of bovine alphaA crystallin (AAC(59-163)) and human alphaB crystallin (ABC(68-162)), both containing the C-terminal extension that functions in chaperone action and oligomeric assembly. In both structures, the C-terminal extensions swap into neighboring molecules, creating runaway domain swaps. This interface, termed DS, enables crystallin polydispersity because the C-terminal extension is palindromic and thereby allows the formation of equivalent residue interactions in both directions. That is, we observe that the extension binds in opposite directions at the DS interfaces of AAC(59-163) and ABC(68-162). A second dimeric interface, termed AP, also enables polydispersity by forming an antiparallel beta sheet with three distinct registration shifts. These two polymorphic interfaces enforce polydispersity of alpha crystallin. This evolved polydispersity suggests molecular mechanisms for chaperone action and for prevention of crystallization, both necessary for transparency of eye lenses. PubMed: 20440841DOI: 10.1002/pro.380 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.15 Å) |
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