2RRH

NMR structure of vasoactive intestinal peptide in Methanol

2RRH の概要

• エントリーDOI: 10.2210/pdb2rrh/pdb
• NMR情報: BMRB: 11419
• 分子名称: VIP peptides (1 entity in total)
• 機能のキーワード: peptide hormone, hormone
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3389.88

構造登録者

Umetsu, Y.,Tenno, T.,Goda, N.,Ikegami, T.,Hiroaki, H. (登録日: 2010-11-12, 公開日: 2011-04-06, 最終更新日: 2024-05-01)

主引用文献

Umetsu, Y.,Tenno, T.,Goda, N.,Shirakawa, M.,Ikegami, T.,Hiroaki, H.
Structural difference of vasoactive intestinal peptide in two distinct membrane-mimicking environments.
Biochim.Biophys.Acta, 1814:724-730, 2011

PubMed Abstract: Vasoactive intestinal peptide (VIP) is a 28-amino acid neuropeptide which belongs to a glucagon/secretin superfamily, the ligand of class II G protein-coupled receptors. Knowledge for the conformation of VIP bound to membrane is important because the receptor activation is initiated by membrane binding of VIP. We have previously observed that VIP-G (glycine-extended VIP) is unstructured in solution, as evidenced by the limited NMR chemical shift dispersion. In this study, we determined the three-dimensional structures of VIP-G in two distinct membrane-mimicking environments. Although these are basically similar structures composed of a disordered N-terminal region and a long α-helix, micelle-bound VIP-G has a curved α-helix. The side chains of residues Phe(6), Tyr(10), Leu(13), and Met(17) found at the concave face form a hydrophobic patch in the micelle-bound state. The structural differences in two distinct membrane-mimicking environments show that the micelle-bound VIP-G localized at the water-micelle boundary with these side chains toward micelle interior. In micelle-bound PACAP-38 (one of the glucagon/secretin superfamily peptide) structure, the identical hydrophobic residues form the micelle-binding interface. This result suggests that these residues play an important role for the membrane binding of VIP and PACAP.

PubMed: 21439408
DOI: 10.1016/j.bbapap.2011.03.009

実験手法

SOLUTION NMR