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

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
585
Issue
2
Identifiers
DOI: 10.1016/j.febslet.2010.12.011
Keywords
  • Glucagon-Like Peptide-2
  • Hormone
  • Nuclear Magnetic Resonance
  • Gpcr
  • Docking
  • Short Bowel Syndrome
Disciplines
  • Medicine

Abstract

Abstract 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 α-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.

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