1GME
Crystal structure and assembly of an eukaryotic small heat shock protein
1GME の概要
| エントリーDOI | 10.2210/pdb1gme/pdb |
| 分子名称 | HEAT SHOCK PROTEIN 16.9B (2 entities in total) |
| 機能のキーワード | small heat shock protein, chaperone, alpha-crystallin |
| 由来する生物種 | TRITICUM AESTIVUM (WHEAT) |
| 細胞内の位置 | Cytoplasm : Q41560 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 67524.67 |
| 構造登録者 | Van Montfort, R.L.M.,Basha, E.,Friedrich, K.L.,Slingsby, C.,Vierling, E. (登録日: 2001-09-13, 公開日: 2001-11-29, 最終更新日: 2024-05-08) |
| 主引用文献 | Van Montfort, R.L.M.,Basha, E.,Friedrich, K.L.,Slingsby, C.,Vierling, E. Crystal Structure and Assembly of an Eukaryotic Small Heat Shock Protein Nat.Struct.Biol., 8:1025-, 2001 Cited by PubMed Abstract: The 2.7 A structure of wheat HSP16.9, a member of the small heat shock proteins (sHSPs), indicates how its alpha-crystallin domain and flanking extensions assemble into a dodecameric double disk. The folding of the monomer and assembly of the oligomer are mutually interdependent, involving strand exchange, helix swapping, loose knots and hinged extensions. In support of the chaperone mechanism, the substrate-bound dimers, in temperature-dependent equilibrium with higher assembly forms, have unfolded N-terminal arms and exposed conserved hydrophobic binding sites on the alpha-crystallin domain. The structure also provides a model by which members of the sHSP protein family bind unfolded substrates, which are involved in a variety of neurodegenerative diseases and cataract formation. PubMed: 11702068DOI: 10.1038/NSB722 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.7 Å) |
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