Comparative protein modeling by satisfaction of spatial restraints.
Approximately one third of known protein sequences are related to at least one known protein structure. As a result, an order of magnitude more sequences can be modeled by comparative modeling than there are experimentally determined protein structures. A large fraction of these models has an accuracy approaching that of a low resolution X-ray structure or a medium resolution nuclear magnetic resonance structure. The number of applications where homology modeling has been proven useful is growing rapidly.
Sali
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Rockefeller University, New York, NY 10021-6399, USA. sali@rockvax.rockefeller.edu
D000595:Amino Acid Sequence; D000818:Animals; D053818:Chymases; D003198:Computer Simulation; D018360:Crystallography, X-Ray; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012697:Serine Endopeptidases / Q000737:chemistry; D012984:Software; D053802:Tryptases
D011506:Proteins; C509190:Tpsb2 protein, mouse; D012697:Serine Endopeptidases; C083294:chymase 2; D053818:Chymases; C509222:Tpsab1 protein, mouse; D053802:Tryptases