International Tables for Crystallography

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Protein folds and motifs: representation, comparison and classification
C. Orengo, J. Thornton, L. Holm and C. Sander. International Tables for Crystallography (2006). Vol. F, ch. 23.1, pp. 575-578  [ doi:10.1107/97809553602060000714 ]

Abstract

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.


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About International Tables for Crystallography

International Tables for Crystallography is the definitive resource and reference work for crystallography. The multi-volume series comprises articles and tables of data relevant to crystallographic research and to applications of crystallographic methods in all sciences concerned with the structure and properties of materials.