ADVANCES IN COMPARATIVE PROTEIN-STRUCTURE MODELING

Comparative modelling of protein 3D structure can now be applied with reasonable accuracy to ten times more protein sequences than the numbe r of experimentally determined protein structures. A protein sequence that has at least 40% identity to a known structure can be modelled au tomatically with an accuracy approaching that of a low resolution X-ra y structure or a medium resolution NMR structure. Currently, the error s in comparative models include mistakes in the packing of sidechains, in the conformation and shifts of the core segments and loops, and, m ost importantly, in an incorrect alignment of the modelled sequence wi th related known structures. Nevertheless, the number of applications in which comparative modelling has been proven to be useful has grown rapidly.