1HTV

CRYSTAL STRUCTURE OF DESTRIPEPTIDE (B28-B30) INSULIN

1HTV の概要

• エントリーDOI: 10.2210/pdb1htv/pdb
• 分子名称: INSULIN, ZINC ION, ... (4 entities in total)
• 機能のキーワード: helix, beta sheet, hormone-growth factor complex, hormone/growth factor
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 33006.92

構造登録者

Ye, J.,Chang, W.,Liang, D. (登録日: 2001-01-01, 公開日: 2001-05-23, 最終更新日: 2024-04-03)

主引用文献

Ye, J.,Chang, W.,Liang, D.
Crystal structure of destripeptide (B28-B30) insulin: implications for insulin dissociation.
Biochim.Biophys.Acta, 1547:18-25, 2001

PubMed Abstract: Destripeptide (B28-B30) insulin (DTRI) is an insulin analogue that has much weaker association ability than native insulin but keeps most of its biological activity. It can be crystallized from a solution containing zinc ions at near-neutral pH. Its crystal structure has been determined by molecular replacement and refined at 1.9 A resolution. DTRI in the crystal exists as a loose hexamer compared with 2Zn insulin. The hexamer only contains one zinc ion that coordinates to the B10 His residues of three monomers. Although residues B28-B30 are located in the monomer-monomer interface within a dimer, the removal of them can simultaneously weaken both the interactions between monomers within the dimer and the interactions between dimers. Because the B-chain C-terminus of insulin is very flexible, we take the DTRI hexamer as a transition state in the native insulin dissociation process and suggest a possible dissociation process of the insulin hexamer based on the DTRI structure.

PubMed: 11343787
DOI: 10.1016/S0167-4838(01)00160-1

実験手法

X-RAY DIFFRACTION (1.9 Å)