1T5Q
Solution Structure of GIP(1-30)amide in TFE/Water
Summary for 1T5Q
| Entry DOI | 10.2210/pdb1t5q/pdb |
| NMR Information | BMRB: 6245 |
| Descriptor | Gastric inhibitory polypeptide (1 entity in total) |
| Functional Keywords | gip, molecular modelling, helix, diabetes, obesity, hormone-growth factor complex, hormone/growth factor |
| Cellular location | Secreted: P09681 |
| Total number of polymer chains | 1 |
| Total formula weight | 3535.95 |
| Authors | Alana, I.,Hewage, C.M.,Malthouse, J.P.G.,Parker, J.C.,Gault, V.A.,O'Harte, F.P.M. (deposition date: 2004-05-05, release date: 2004-11-16, Last modification date: 2024-05-22) |
| Primary citation | 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 Cited by 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: 15522230DOI: 10.1016/j.bbrc.2004.10.033 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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