title: Three-dimensional structure of an alpha-amylase inhibitor HAIM as determined by nuclear magnetic resonance methods.
abstract: The three-dimensional structure of an alpha-amylase inhibitor, HAIM, composed of 78 amino acids, was analyzed by two-dimensional NMR techniques. Sequence-specific assignments were made for the amino acid residues from Ile-6 to Cys-72. Distance geometry analysis of the interresidue NOEs revealed that the HAIM molecule consists of two beta-sheets, as is the case in a homologous alpha-amylase inhibitor, Tendamistat, though one of its beta-strands is much shorter than that of Tendamistat. The combination of molecular modeling from Tendamistat and distance geometry analysis was confirmed to be useful for our purpose.
authors.affiliation: Protein Engineering Research Institute, Osaka.
authors.forename: M
authors.initials: M
authors.lastname: Yoshida
authors.forename: T
authors.initials: T
authors.lastname: Nakai
authors.forename: K
authors.initials: K
authors.lastname: Fukuhara
authors.forename: S
authors.initials: S
authors.lastname: Saitoh
authors.forename: W
authors.initials: W
authors.lastname: Yoshikawa
authors.forename: Y
authors.initials: Y
authors.lastname: Kobayashi
authors.forename: H
authors.initials: H
authors.lastname: Nakamura
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D013302:Streptomyces / Q000032:analysis; D000516:alpha-Amylases / Q000037:antagonists & inhibitors*
chemical_list: D001426:Bacterial Proteins; C051225:HaimII protein, Streptomyces griseosporeus; D010455:Peptides; D000516:alpha-Amylases; C030526:tendamistate