1GCN
X-RAY ANALYSIS OF GLUCAGON AND ITS RELATIONSHIP TO RECEPTOR BINDING
Summary for 1GCN
Entry DOI | 10.2210/pdb1gcn/pdb |
Descriptor | GLUCAGON (1 entity in total) |
Functional Keywords | hormone |
Biological source | Sus scrofa (pig) |
Cellular location | Secreted: P01274 |
Total number of polymer chains | 1 |
Total formula weight | 3486.78 |
Authors | Blundell, T.L.,Sasaki, K.,Dockerill, S.,Tickle, I.J. (deposition date: 1977-10-17, release date: 1977-11-28, Last modification date: 2024-02-07) |
Primary citation | Sasaki, K.,Dockerill, S.,Adamiak, D.A.,Tickle, I.J.,Blundell, T. X-ray analysis of glucagon and its relationship to receptor binding. Nature, 257:751-757, 1975 Cited by PubMed Abstract: X-ray analysis of the pancreatic hormone glucagon shows that in crystals the polypeptide adopts a mainly helical conformation, which is stabilised by hydrophobic interactions between molecules related by threefold symmetry. A model is presented in which the glucagon molecule exists in dilute solutions as an equilibrium population of conformers with little retention of conformers with little retention of structure, and in which the helical conformation is stablised by hydrophobic interactions either as an oligomer or as a complex with the receptor. PubMed: 171582DOI: 10.1038/257751a0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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