2HIU

NMR STRUCTURE OF HUMAN INSULIN IN 20% ACETIC ACID, ZINC-FREE, 10 STRUCTURES

「1HIU」から置き換えられました

2HIU の概要

• エントリーDOI: 10.2210/pdb2hiu/pdb
• 分子名称: INSULIN (2 entities in total)
• 機能のキーワード: insulin, hormone, glucose metabolism
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Secreted: P01308 P01308
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 5817.65

構造登録者

Hua, Q.X.,Gozani, S.N.,Chance, R.E.,Hoffmann, J.A.,Frank, B.H.,Weiss, M.A. (登録日: 1996-10-08, 公開日: 1997-04-01, 最終更新日: 2024-10-23)

主引用文献

Hua, Q.X.,Gozani, S.N.,Chance, R.E.,Hoffmann, J.A.,Frank, B.H.,Weiss, M.A.
Structure of a protein in a kinetic trap.
Nat.Struct.Biol., 2:129-138, 1995

PubMed Abstract: We have determined the structure of a metastable disulphide isomer of human insulin. Although not observed for proinsulin folding or insulin-chain recombination, the isomer retains ordered secondary structure and a compact hydrophobic core. Comparison with native insulin reveals a global rearrangement in the orientation of A- and B-chains. One face of the protein's surface is nevertheless in common between native and non-native structures. This face contains receptor-binding determinants, rationalizing the partial biological activity of the isomer. Structures of native and non-native disulphide isomers also define alternative three-dimensional templates. Threading of insulin-like sequences provide an experimental realization of the inverse protein-folding problem.

PubMed: 7749917
DOI: 10.1038/nsb0295-129

実験手法

SOLUTION NMR