1LYY

AMYLOIDOGENIC VARIANT (ASP67HIS) OF HUMAN LYSOZYME

1LYY の概要

• エントリーDOI: 10.2210/pdb1lyy/pdb
• 分子名称: LYSOZYME (2 entities in total)
• 機能のキーワード: hydrolase, enzyme, beta-1, 4-glycan-hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P61626
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14743.75

構造登録者

Sunde, M.,Blake, C.C.F. (登録日: 1997-01-16, 公開日: 1997-04-01, 最終更新日: 2024-11-20)

主引用文献

Booth, D.R.,Sunde, M.,Bellotti, V.,Robinson, C.V.,Hutchinson, W.L.,Fraser, P.E.,Hawkins, P.N.,Dobson, C.M.,Radford, S.E.,Blake, C.C.,Pepys, M.B.
Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis.
Nature, 385:787-793, 1997

PubMed Abstract: Tissue deposition of soluble proteins as amyloid fibrils underlies a range of fatal diseases. The two naturally occurring human lysozyme variants are both amyloidogenic, and are shown here to be unstable. They aggregate to form amyloid fibrils with transformation of the mainly helical native fold, observed in crystal structures, to the amyloid fibril cross-beta fold. Biophysical studies suggest that partly folded intermediates are involved in fibrillogenesis, and this may be relevant to amyloidosis generally.

PubMed: 9039909
DOI: 10.1038/385787a0

実験手法

X-RAY DIFFRACTION (1.8 Å)