title: Crystal structure determination, refinement and the molecular model of the alpha-amylase inhibitor Hoe-467A.
abstract: The crystal and molecular structure of the alpha-amylase inhibitor Hoe-467A has been determined and refined at high resolution. The polypeptide chain is folded in two triple-stranded sheets, which form a barrel. The topology of folding is as found in the immunoglobulin domains. The amino acid triplet Trp18-Arg19-Tyr20 has an exceptional conformation and position in the molecule and is possibly involved in inhibitory activity.
mesh_terms: D000595:Amino Acid Sequence; D008958:Models, Molecular; D010455:Peptides; D011487:Protein Conformation; D014961:X-Ray Diffraction; D000516:alpha-Amylases / Q000037:antagonists & inhibitors*
chemical_list: D010455:Peptides; D000516:alpha-Amylases; C030526:tendamistate