Conformational and molecular interaction studies of glucagon-like peptide-2 with its N-terminal extracellular receptor domain |
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Authors: | Venneti Kalyana C Hewage Chandralal M |
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Institution: | School of Biomolecular and Biomedical Science, Centre for Synthesis and Chemical Biology, SEC Strategic Research Cluster, UCD Conway Institute, University College Dublin, Dublin 4, Ireland |
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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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Keywords: | Glucagon-like peptide-2 Hormone Nuclear magnetic resonance GPCR Docking Short bowel syndrome |
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