Comparative modelling allows each experimentally
determined fold to provide structure information for a
family of related proteins94. The quality of the model
can range from extremely good to virtually worthless,
depending on the intended use and the evolutionary
distance between the template (solved structure) and
the query, in large part because of problems with alignment95,96.
Because the structural information of most
proteins will be available only as a homology model,
understanding the strengths and limitations of the comparative
modelling methods will be crucial for making
informed use of structural genomics data.