Conserved Features in the Active Site of Nonhomologous Serine Proteases

This project, supported by NIH NLM-05652, NLM-06244 and the Culpeper Foundation, is part of the Helix Group at the Stanford Section on Medical Informatics. Please address inquiries to altman@smi.stanford.edu.
This work is published in Folding & Design, in press.

Conserved Features in the Active Site of Nonhomologous Serine Proteases

Bagley, S.C. and Altman, R.B.

Shared Data

We have created a kinemage file, using the MAGE program, that allows viewing of the four superimposed serine proteases used in this study: 1TLD, 1EAP, 1ST3, and the mirror image of wheat serine carboxypeptidase complexed to chymostatin (submitted to PDB). In addition, the kinemage allows different biophysical and biochemical properties to be toggled on and off. When toggled "on" a set of colored spheres are displayed in the volumes in which the features were observed to be significantly abundant in the protease molecules studied. In addition, the text fields of the kinemage provide the raw data for the four proteases (the "sites") and the 19 control histidines (the "nonsites").
  1. The kinemage file can be downloaded here
  2. The MAGE program for Macintosh (in stuff'ed and binhex'ed form) is here.
  3. The MAGE program for PC computeres is here.

    Last update July, 1996. altman@smi.stanford.edu