1t5q

Publication Abstract from PubMed

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.

NMR structure of the glucose-dependent insulinotropic polypeptide fragment, GIP(1-30)amide.,Alana I, Hewage CM, Malthouse JP, Parker JC, Gault VA, O'Harte FP Biochem Biophys Res Commun. 2004 Dec 3;325(1):281-6. PMID:15522230^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.