Prediction of tertiary structures in 'scorpion-toxin' type proteins.
In the three-dimensional architecture of macromolecules, the structural stability and proper folding manifest due to cooperative packing interaction of various segments. Hydrophobicity is the major factor stabilizing protein-protein associations. In the disulfide-containing proteins, S-S bonds are integral part of structural motifs and large part of the protein-folding problem can be reduced to identifying and understanding motifs and subdomains of these proteins. Identifying such a motif with S-S bonds in 'scorpion-toxin' type proteins, and from model-building studies, five tertiary structural models for these type of proteins can be proposed. These canonical structural models can be refined by regular minimum energy and computer simulation methods to arrive at the final tertiary structures. Such 'models' can be of considerable use i) in understanding the biochemical reaction mechanisms in the structure-function relationships, ii) structure determination by X-ray methods (molecular replacement method), iii) drug design etc.
Narayanan
P
P
Department of Life Sciences, University of Bombay, India.
Lala
K
K
D000595:Amino Acid Sequence; D000818:Animals; D004220:Disulfides / Q000737:chemistry; D008969:Molecular Sequence Data; D009498:Neurotoxins / Q000737:chemistry*; D011487:Protein Conformation; D012604:Scorpion Venoms / Q000737:chemistry*; D016415:Sequence Alignment
D004220:Disulfides; D009498:Neurotoxins; D012604:Scorpion Venoms