1FB9

EFFECTS OF S-SULFONATION ON THE SOLUTION STRUCTURE OF SALMON CALCITONIN

1FB9 の概要

• エントリーDOI: 10.2210/pdb1fb9/pdb
• 関連するPDBエントリー: 1BKU 1BYV 1BZB
• 分子名称: CALCITONIN ANALOGUE (1 entity in total)
• 機能のキーワード: alpha helix, signaling protein
• 由来する生物種: Oncorhynchus gorbuscha (pink salmon)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3597.02

構造登録者

Wu, H.,Mao, J.,Wang, Y.,Dou, H. (登録日: 2000-07-14, 公開日: 2003-07-01, 最終更新日: 2018-06-27)

主引用文献

Wang, Y.,Dou, H.,Cao, C.,Zhang, N.,Ma, J.,Mao, J.,Wu, H.
Solution structure and biological activity of recombinant salmon calcitonin S-sulfonated analog
Biochem.Biophys.Res.Commun., 306:582-589, 2003

PubMed Abstract: Salmon calcitonin S-sulfonated analog (abbreviated as [S-SO(3)(-)]rsCT) was prepared by introducing two sulfonic groups into the side chains of Cys1 and Cys7 of recombinant salmon calcitonin. The hypocalcemic potency of this open-chain analog is 5500IU/mg, which is about 30% higher than that (4500IU/mg) of the wild type. The solution conformation of [S-SO(3)(-)]rsCT was studied in aqueous trifluoroethanol solution by CD, 2D-NMR spectroscopy, and distance geometry calculations. In the mixture of 60% TFE and 40% water, the peptide assumes an amphipathic alpha-helix in the region of residues 4-22, which is one turn longer than that of the native sCT. The structural feature analysis of the peptide revealed the presence of hydrophobic surface composed of five hydrophobic side chains of residues Leu4, Leu9, Leu12, Leu16, and Leu19, and a network of salt-bridges that consisted of a tetrad of oppositely charged side chains (Cys7-SO(3)(-)-Lys11(+)-Glu15(-)-Lys18(+)). The multiple salt bridges resulted in the stabilization of the longer amphipathic alpha-helix. Meanwhile, the higher hypocalcemic potency of the peptide could be attributed to the array of hydrophobic side chains of five leucine residues of the amphipathic alpha-helix.

PubMed: 12804605
DOI: 10.1016/S0006-291X(03)01028-3

実験手法

SOLUTION NMR