2QIU

Structure of Human Arg-Insulin

2QIU の概要

• エントリーDOI: 10.2210/pdb2qiu/pdb
• 関連するPDBエントリー: 1ZNI
• 分子名称: Insulin, ZINC ION, ... (4 entities in total)
• 機能のキーワード: hormone, glucose utilisation, t3r3 conformation
• 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: 4
• 化学式量合計: 12080.51

構造登録者

Sreekanth, R.,Pattabhi, V.,Rajan, S.S. (登録日: 2007-07-05, 公開日: 2008-02-26, 最終更新日: 2024-11-20)

主引用文献

Sreekanth, R.,Pattabhi, V.,Rajan, S.S.
Structural interpretation of reduced insulin activity as seen in the crystal structure of human Arg-insulin
Biochimie, 90:467-473, 2008

PubMed Abstract: The N-terminal glycine of the A-chain in insulin is reported to be one of the residues that binds to the insulin receptor. Modifications near this region lead to variations in the biological activity of insulin. One such modification viz., an addition of an arginine at the N-terminal A-chain, was reported to possess two-thirds the activity of native insulin. The crystal structure of 2 zinc human arg (A0) insulin has been elucidated to 2A resolution to understand the mechanism of reduction in insulin activity. A conformational transition from T6 to T3R3(f) and a decrease in the surface accessibility of residues in the so called receptor binding region have been observed. The presence of arginine has also induced distortions in the A chain N-terminal helix. The subtle conformational alterations like decrease in surface accessibility, alterations in the charge surface and changes in the relative orientation of the two helices in the A chain may be responsible for the reduction in activity.

PubMed: 18029081
DOI: 10.1016/j.biochi.2007.09.012

実験手法

X-RAY DIFFRACTION (2 Å)