A secondary structure prediction of the hemorrhagic metalloprotease family.
A secondary structure has been predicted for the hemorrhagic metalloproteases using a method developed in Zurich that extracts structural information from patterns of conservation and variation in homologous protein sequences. This prediction tests the limits of the method when applied to a small number of homologous sequences that have undergone only modest evolutionary divergence. Predictions were also obtained using a neural network developed by Sander and coworkers, to date the best fully automated method for predicting secondary structure, and using the classical Chou-Fasman and GOR heuristics. The predictions are different. No crystal structure is known within this protein family, but one is expected shortly. Therefore, this prediction should contribute significantly to the evaluation of the relative merits of these prediction methods.
Gerloff
D L
DL
Laboratory for Organic Chemistry, E.T.H. Zurich, Switzerland.
Jenny
T F
TF
Knecht
L J
LJ
Benner
S A
SA
D000595:Amino Acid Sequence; D000818:Animals; D006470:Hemorrhage; D008666:Metalloendopeptidases / Q000737:chemistry* / Q000633:toxicity; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D012910:Snake Venoms / Q000633:toxicity*
D012910:Snake Venoms; D008666:Metalloendopeptidases