title: Antiparallel beta-sheets in the crystal structure of the heptapeptide Met-Glu-His-Phe-Arg-Trp-Gly (ACTH 4-10).
abstract: The conformation of the molecules in ACTH 4-10 has been determined as part of a study of the conformations of the biologically active N-terminal fragments of the adrenocorticotropic hormone (ACTH). ACTH 4-10 crystallizes in two different superstructures. The substructure considered in the present work, is monoclinic, space group C2, a = 25.75(1) A, b = 27.78(1) A, c = 20.35(1) A, beta = 114.0(1) degrees, Z = 8 molecules ACTH 4-10 plus 22 weight per cent solvent. The crystals contain antiparallel beta-sheets, the orientations of the side groups are not found, because of disorder. The present crystal structure and those of other linear oligopeptides emphasize that antiparallel beta-sheets are energetically favourable. It is very unlikely, however, that the ACTH 4-10 crystals contain the molecules in their biologically active form.
mesh_terms: D000324:Adrenocorticotropic Hormone; D008958:Models, Molecular; D010446:Peptide Fragments; D011487:Protein Conformation; D014961:X-Ray Diffraction
chemical_list: D010446:Peptide Fragments; D000324:Adrenocorticotropic Hormone; C011394:ACTH (4-10)