|
The X-ray crystal structure of Streptomyces griseus trypsin has been solved and
refined at 1.7-A resolution. The structure of this protein had been predicted in
two models on the basis of its expected homology to structures of bovine trypsin
and other pancreatic serine proteases [Jurásek, L., Olafson, R.W., Johnson, P.,
& Smillie, L.B. (1976) Miami Winter Symp. 11, 93-123; Greer, J. (1981) J.
Mol. Biol. 153, 1027-1042]. An evaluation of these models in light of the known
structure demonstrates the effect of several sources of error on such
comparative model building. The objective of comparative model building is often
to explain substrate specificity, or to suggest potential highly specific drugs.
The unique parts of modeled proteins that are most important for such purposes
are, however, the most poorly determined by the model-building procedure.
|
