7RJ07RJ0 の概要
| エントリーDOI | 10.2210/pdb7rj0/pdb |
| 分子名称 | Gamma-crystallin S (2 entities in total) |
| 機能のキーワード | octamer, domain-swap, oxidation, disorder, protein binding, structural protein |
| 由来する生物種 | Mus musculus (Mouse) |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 83679.52 |
| 構造登録者 | |
| 主引用文献 | Sagar, V.,Wistow, G. Acquired Disorder and Asymmetry in a Domain-Swapped Model for gamma-Crystallin Aggregation. J.Mol.Biol., 434:167559-167559, 2022 Cited by PubMed Abstract: Misfolding and aggregation of proteins occur in many pathological states. Because of the inherent disorder involved, these processes are difficult to study. We attempted to capture aggregation intermediates of γS-crystallin, a highly stable, internally symmetrical monomeric protein, by crystallization under mildly acidic and oxidizing conditions. Here we describe novel oligomerization through strained domain-swapping and partial intermolecular disulfide formation. This forms an octamer built from asymmetric tetramers, each of which comprises an asymmetric pair of twisted, domain-swapped dimers. Each tetramer shows patterns of acquired disorder among subunits, ranging from local loss of secondary structure to regions of intrinsic disorder. The octamer ring is tied together by partial intermolecular disulfide bonds, which may contribute to strain and disorder in the octamer. Oligomerization in this structure is self-limited by the distorted octamer ring. In a more heterogeneous environment, the disordered regions could serve as seeds for cascading interactions with other proteins. Indeed, solubilized protein from crystals retain many features observed in the crystal and are prone to further oligomerization and precipitation. This structure illustrates modes of loss of organized structure and aggregation that are relevant for cataract and for other disorders involving deposition of formerly well-folded proteins. PubMed: 35341744DOI: 10.1016/j.jmb.2022.167559 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.919 Å) |
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