4.5 Article

Conformational and molecular interaction studies of glucagon-like peptide-2 with its N-terminal extracellular receptor domain

Journal

FEBS LETTERS
Volume 585, Issue 2, Pages 346-352

Publisher

WILEY
DOI: 10.1016/j.febslet.2010.12.011

Keywords

Glucagon-like peptide-2; Hormone; Nuclear magnetic resonance; GPCR; Docking; Short bowel syndrome

Funding

  1. Science Foundation Ireland [06/RFP/CHO006]
  2. Science Foundation Ireland (SFI) [06/RFP/CHO006] Funding Source: Science Foundation Ireland (SFI)

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Glucagon-like peptide-2 (GLP-2) is a therapeutic target used in the treatment of short bowel syndrome. In this paper, we present the three dimensional solution structure of GLP-2 peptide determined using nuclear magnetic resonance (NMR) and molecular modelling. The GLP-2 adopts an a-helical conformation similar to that of secretin family of hormones. In order to understand the molecular details governing the ligand binding and receptor activation, macromolecular docking studies were performed between the N-terminal extracellular domain of GLP-2 receptor and the GLP-2 hormone using a data driven docking program. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

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