1GEA

RECEPTOR-BOUND CONFORMATION OF PACAP21

1GEA の概要

• エントリーDOI: 10.2210/pdb1gea/pdb
• NMR情報: BMRB: 4916
• 分子名称: PITUITARY ADENYLATE CYCLASE ACTIVATING POLYPEPTIDE (1 entity in total)
• 機能のキーワード: beta coil, consecutive beta turns, type-ii beta turn, type-i beta turn, helix, neuropeptide
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2522.88

構造登録者

Inooka, H.,Ohtaki, T.,Kitahara, O.,Ikegami, T.,Endo, S.,Kitada, C.,Ogi, K.,Onda, H.,Fujino, M.,Shirakawa, M. (登録日: 2000-10-20, 公開日: 2001-04-20, 最終更新日: 2023-12-27)

主引用文献

Inooka, H.,Ohtaki, T.,Kitahara, O.,Ikegami, T.,Endo, S.,Kitada, C.,Ogi, K.,Onda, H.,Fujino, M.,Shirakawa, M.
Conformation of a peptide ligand bound to its G-protein coupled receptor.
Nat.Struct.Biol., 8:161-165, 2001

PubMed Abstract: Many peptide hormones elicit a wide array of physiological effects by binding to G-protein coupled receptors. We have determined the conformation of pituitary adenylate cyclase activating polypeptide, PACAP(1--21)NH(2), bound to a PACAP-specific receptor by NMR spectroscopy. Residues 3--7 form a unique beta-coil structure that is preceded by an N-terminal extended tail. This beta-coil creates a patch of hydrophobic residues that is important for receptor binding. In contrast, the C-terminal region (residues 8--21) forms an alpha-helix, similar to that in the micelle-bound PACAP. Thus, the conformational difference between PACAP in the receptor-bound and the micelle-bound states is limited to the N-terminal seven residues. This observation is consistent with the two-step ligand transportation model in which PACAP first binds to the membrane nonspecifically and then diffuses two-dimensionally in search of its receptor; a conformational change at the N-terminal region then allows specific interactions between the ligand and the receptor.

PubMed: 11175907
DOI: 10.1038/84159

実験手法

SOLUTION NMR