2L63
NMR solution structure of GLP-2 in 2,2,2 trifluroethanol
Summary for 2L63
| Entry DOI | 10.2210/pdb2l63/pdb |
| Related | 2L64 |
| NMR Information | BMRB: 17296 |
| Descriptor | Glucagon-like peptide 2 (1 entity in total) |
| Functional Keywords | glp-2, hormone, gpcr, docking, small bowel syndrome |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted: P01275 |
| Total number of polymer chains | 1 |
| Total formula weight | 3769.14 |
| Authors | Venneti, K.C.,Hewage, C.M. (deposition date: 2010-11-12, release date: 2011-02-23, Last modification date: 2024-05-01) |
| Primary citation | Venneti, K.C.,Hewage, C.M. Conformational and molecular interaction studies of glucagon-like peptide-2 with its N-terminal extracellular receptor domain. Febs Lett., 585:346-352, 2011 Cited by PubMed 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. PubMed: 21167157DOI: 10.1016/j.febslet.2010.12.011 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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