Chapter 23.1 Protein folds and motifs: representation, comparison and classification
Crystallography of biological macromolecules
First Online Edition (2006)
Part 23. Structural analysis and classification
Published Online: 1 JAN 2006
© International Union of Crystallography 2006
International Tables for Crystallography
How to Cite
Orengo, C., Thornton, J., Holm, L. and Sander, C. 2006. Protein folds and motifs: representation, comparison and classification. International Tables for Crystallography. 575–578.
- Published Online: 1 JAN 2006
The assignment of protein domains from three-dimensional structure is critically important in understanding protein evolution and function. Domains are quasi-independent substructures that are thought to fold autonomously, to carry specific molecular functions, to move relative to each other as semi-rigid bodies and to speed the evolution of new functions by recombination. In the first part of this chapter, the classification of protein folds is discussed. In the second part of the chapter, the concepts underlying computational methods for locating domains in 3D structures are presented. Early algorithms focused on physical criteria to identify compact subunits. With the growth of the structural database, the focus has shifted to methods for identifying recurrent substructures that can form the basis for a consistent protein-structure classification.
- protein domains;
- protein structure classification