1EV6

Structure of the monoclinic form of the M-cresol/insulin R6 hexamer

1EV6 の概要

• エントリーDOI: 10.2210/pdb1ev6/pdb
• 関連するPDBエントリー: 1EV3
• 分子名称: INSULIN, M-CRESOL, ZINC ION, ... (7 entities in total)
• 機能のキーワード: r6 hexameric insulin, hormone-growth factor complex, hormone/growth factor
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 35887.59

構造登録者

Smith, G.D.,Ciszak, E.,Magrum, L.A.,Pangborn, W.A.,Blessing, R.H. (登録日: 2000-04-19, 公開日: 2000-12-04, 最終更新日: 2024-10-30)

主引用文献

Smith, G.D.,Ciszak, E.,Magrum, L.A.,Pangborn, W.A.,Blessing, R.H.
R6 Hexameric Insulin Complexed with m-Cresol or Resorcinol
Biochem.Biophys.Res.Commun., 56:1541-1548, 2000

PubMed Abstract: The structures of three R(6) human insulin hexamers have been determined. Crystals of monoclinic m-cresol-insulin, monoclinic resorcinol-insulin and rhombohedral m-cresol-insulin diffracted to 1. 9, 1.9 and 1.78 A, respectively, and have been refined to residuals of 0.195, 0.179 and 0.200, respectively. In all three structures, a phenolic derivative is found to occupy the phenolic binding site, where it forms hydrogen bonds to the carbonyl O atom of CysA6 and the N atom of CysA11. Two additional phenolic derivative binding sites were identified within or between hexamers. The structures of all three hexamers are nearly identical, although a large displacement of the N-terminus of one B chain in both monoclinic structures results from coordination to a sodium ion which is located between symmetry-related hexamers. Other minor differences in structure arise from differences in packing in the monoclinic cell compared with the rhombohedral cell. Based upon the differences in conformation of the GluB13 side chains in T(6), T(3)R(f)(3) and R(6) hexamers, the deprotonation of these side chains appears to be associated with the T-->R conformational transition.

PubMed: 11092919
DOI: 10.1107/S0907444900012749

実験手法

X-RAY DIFFRACTION (1.9 Å)