1T5Q

Solution Structure of GIP(1-30)amide in TFE/Water

1T5Q の概要

• エントリーDOI: 10.2210/pdb1t5q/pdb
• NMR情報: BMRB: 6245
• 分子名称: Gastric inhibitory polypeptide (1 entity in total)
• 機能のキーワード: gip, molecular modelling, helix, diabetes, obesity, hormone-growth factor complex, hormone/growth factor
• 細胞内の位置: Secreted: P09681
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3535.95

構造登録者

Alana, I.,Hewage, C.M.,Malthouse, J.P.G.,Parker, J.C.,Gault, V.A.,O'Harte, F.P.M. (登録日: 2004-05-05, 公開日: 2004-11-16, 最終更新日: 2024-05-22)

主引用文献

Alana, I.,Hewage, C.M.,Malthouse, J.P.G.,Parker, J.C.,Gault, V.A.,O'Harte, F.P.M.
NMR structure of the glucose-dependent insulinotropic polypeptide fragment, GIP(1-30)amide.
Biochem.Biophys.Res.Commun., 325:281-286, 2004

PubMed Abstract: Glucose-dependent insulinotropic polypeptide is an incretin hormone that stimulates insulin secretion and reduces postprandial glycaemic excursions. The glucose-dependent action of GIP on pancreatic beta-cells has attracted attention towards its exploitation as a potential drug for type 2 diabetes. Use of NMR or X-ray crystallography is vital to determine the three-dimensional structure of the peptide. Therefore, to understand the basic structural requirements for the biological activity of GIP, the solution structure of the major biologically active fragment, GIP(1-30)amide, was investigated by proton NMR spectroscopy and molecular modelling. The structure is characterised by a full length alpha-helical conformation between residues F(6) and A(28). This structural information could play an important role in the design of therapeutic agents based upon GIP receptor agonists.

PubMed: 15522230
DOI: 10.1016/j.bbrc.2004.10.033

実験手法

SOLUTION NMR