1V6R

Solution Structure of Endothelin-1 with its C-terminal Folding

1V6R の概要

• エントリーDOI: 10.2210/pdb1v6r/pdb
• NMR情報: BMRB: 6070
• 分子名称: Endothelin-1 (1 entity in total)
• 機能のキーワード: endothelin, a-helix, c-terminal folding, cardiovascular bioactive peptide, g-protein coupled-receptor ligand, contractile protein
• 細胞内の位置: Secreted: P05305
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2497.95

構造登録者

Takashima, H.,Mimura, N.,Ohkubo, T.,Yoshida, T.,Tamaoki, H.,Kobayashi, Y. (登録日: 2003-12-03, 公開日: 2004-03-16, 最終更新日: 2024-10-30)

主引用文献

Takashima, H.,Mimura, N.,Ohkubo, T.,Yoshida, T.,Tamaoki, H.,Kobayashi, Y.
Distributed Computing and NMR Constraint-Based High-Resolution Structure Determination: Applied for Bioactive Peptide Endothelin-1 To Determine C-Terminal Folding
J.Am.Chem.Soc., 126:4504-4505, 2004

PubMed Abstract: Distributed computing has been implemented to the solution structure determination of endothelin-1 to evaluate efficiency of the method for NMR constraint-based structure calculations. A key target of the investigation was determination of the C-terminal folding of the peptide, which had been dispersed in previous studies of NMR, despite its pharmacological significances. With use of tens of thousands of random initial structures to explore the conformational space comprehensively, we determined high-resolution structures with good convergences of C-terminal as well as previously defined N-terminal structures. The previous studies had missed the C-terminal convergence because of initial structure dependencies trapped in localized folding of the N-terminal region, which are strongly constricted by two disulfide bonds.

PubMed: 15070353
DOI: 10.1021/ja031637w

実験手法

SOLUTION NMR