3HYD

LVEALYL peptide derived from human insulin chain B, residues 11-17

3HYD の概要

• エントリーDOI: 10.2210/pdb3hyd/pdb
• 関連するPDBエントリー: 2OMQ
• 分子名称: Insulin (2 entities in total)
• 機能のキーワード: amyloid-like protofibril, carbohydrate metabolism, cleavage on pair of basic residues, diabetes mellitus, disease mutation, disulfide bond, glucose metabolism, hormone, pharmaceutical, secreted, protein fibril
• 細胞内の位置: Secreted: P01308
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 819.99

構造登録者

Ivanova, M.I.,Sawaya, M.R.,Eisenberg, D. (登録日: 2009-06-22, 公開日: 2009-10-06, 最終更新日: 2024-04-03)

主引用文献

Ivanova, M.I.,Sievers, S.A.,Sawaya, M.R.,Wall, J.S.,Eisenberg, D.
Molecular basis for insulin fibril assembly.
Proc.Natl.Acad.Sci.USA, 106:18990-18995, 2009

PubMed Abstract: In the rare medical condition termed injection amyloidosis, extracellular fibrils of insulin are observed. We found that the segment of the insulin B-chain with sequence LVEALYL is the smallest segment that both nucleates and inhibits the fibrillation of full-length insulin in a molar ratio-dependent manner, suggesting that this segment is central to the cross-beta spine of the insulin fibril. In isolation from the rest of the protein, LVEALYL forms microcrystalline aggregates with fibrillar morphology, the structure of which we determined to 1 A resolution. The LVEALYL segments are stacked into pairs of tightly interdigitated beta-sheets, each pair displaying the dry steric zipper interface typical of amyloid-like fibrils. This structure leads to a model for fibrils of human insulin consistent with electron microscopic, x-ray fiber diffraction, and biochemical studies.

PubMed: 19864624
DOI: 10.1073/pnas.0910080106

実験手法

X-RAY DIFFRACTION (1 Å)