J. Biochem, 1990, Vol. 108, No. 2 158-165
© 1990 Japanese Biochemical Society
research-article |
Three-Dimensional Structure of an
-Amylase Inhibitor HAIM as Determined by Nuclear Magnetic Resonance Methods
*Protein Engineering Research Institute Suita, Osaka 565
**Institute for Proyein Research, Osaka University Suita, Osaka 565
1To whom correspondence should be addressed
The three-dimensional structure of an
-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 Iie-6 to Cys-72. Distance geometry analysis of the Interresldue NOEs revealed that the HAIM molecule consists of two ß-sheets, as Is the case In a homologous
-aniylase Inhibitor, Tendamistat, though one of its ß-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.