Part 4. Bioinformatics
4.6. Methods for Structure Analysis and Prediction
Published Online: 15 APR 2005
Copyright © 2005 John Wiley & Sons, Ltd
Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics
How to Cite
Heringa, J. 2005. Protein domains. Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics. 4:4.6:68.
- Published Online: 15 APR 2005
Many cellular processes involve proteins composed of multiple domains. The modular nature afforded by breaking up a protein's three-dimensional structure into discrete domains has many evolutionary advantages. First, it allows proteins to evolve to complex cooperative functions that require elaborate, large, and stable structural scaffolds, which would be impossible to form otherwise within the structural constraints associated with the protein-folding process. Second, it can bring active sites in proximity in a fixed stoichiometric ratio. Third, otherwise unstable intermediates can be accommodated within interdomain clefts. Fourth, the flexibility afforded by protein domain linker regions, for example, hinge regions, can greatly aid the activity of the cooperative catalytic process carried out by a multidomain enzyme. Fifth, the repeated and combinatorial use of domains in multidomain proteins has provided nature both an evolutionary economic and versatile system to maintain and enhance cellular activity.
- domain structure;
- protein module;
- domain motion;
- domain linker;
- domain prediction;
- domain database