X-ray analysis of glucagon and its relationship to receptor binding.
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.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D005934:Glucagon / Q000032:analysis / Q000378:metabolism; D007328:Insulin; D008961:Models, Structural; D010179:Pancreas / Q000378:metabolism; D011487:Protein Conformation; D011956:Receptors, Cell Surface; D012996:Solutions; D013329:Structure-Activity Relationship
D007328:Insulin; D011956:Receptors, Cell Surface; D012996:Solutions; D005934:Glucagon