Sánchez R, Sali A
Box 270, The Rockefeller University 1230 York Avenue, New York, NY 10021-6399, USA.
Curr Opin Struct Biol. 1997 Apr;7(2):206-14. doi: 10.1016/s0959-440x(97)80027-9.
Comparative modelling of protein 3D structure can now be applied with reasonable accuracy to ten times more protein sequences than the number of experimentally determined protein structures. A protein sequence that has at least 40% identity to a known structure can be modelled automatically with an accuracy approaching that of a low resolution X-ray structure or a medium resolution NMR structure. Currently, the errors in comparative models include mistakes in the packing of sidechains, in the conformation and shifts of the core segments and loops, and, most importantly, in an incorrect alignment of the modelled sequence with related known structures. Nevertheless, the number of applications in which comparative modelling has been proven to be useful has grown rapidly.
目前，蛋白质三维结构的比较建模能够以合理的准确度应用于比实验测定的蛋白质结构数量多十倍的蛋白质序列。与已知结构具有至少40% 同一性的蛋白质序列能够以接近低分辨率X射线结构或中等分辨率核磁共振结构的准确度自动建模。目前，比较模型中的误差包括侧链堆积错误、核心片段和环的构象及位移错误，以及最重要的，建模序列与相关已知结构的不正确比对。然而，已证明比较建模有用的应用数量增长迅速。
