Predicting coiled-coil regions in proteins.
The past several years have seen significant advances in our ability to recognize coiled coils from protein sequences and model their structures. New methods include a detection program based on pairwise residue correlations, a program that distinguishes two-stranded from three-stranded coiled coils and a routine for modelling the coordinates of the core residues in coiled coils. Several widely noted predictions, among them those for heterotrimeric G proteins and for cartilage oligomeric matrix protein, have been confirmed by crystal structures, and several new predictions have been made, including a model for the still hypothetical right-handed coiled coil.
Lupas
A
A
Max-Planck-Institut für Biochemie, Martinsried, Germany. lupas@vms.biochem.mpg.de
D003198:Computer Simulation; D018360:Crystallography, X-Ray; D019204:GTP-Binding Proteins / Q000737:chemistry; D008958:Models, Molecular; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012984:Software
D011506:Proteins; D019204:GTP-Binding Proteins