Three-dimensional structure of an alpha-amylase inhibitor HAIM as determined by nuclear magnetic resonance methods.
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.
Yoshida
M
M
Protein Engineering Research Institute, Osaka.
Nakai
T
T
Fukuhara
K
K
Saitoh
S
S
Yoshikawa
W
W
Kobayashi
Y
Y
Nakamura
H
H
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*
D001426:Bacterial Proteins; C051225:HaimII protein, Streptomyces griseosporeus; D010455:Peptides; D000516:alpha-Amylases; C030526:tendamistate