Protein folds: molecular systematics in three dimensions

Citation
C. Zhang et C. Delisi, Protein folds: molecular systematics in three dimensions, CELL MOL L, 58(1), 2001, pp. 72-79
Citations number
60
Language
INGLESE
art.tipo
Review
Categorie Soggetti
Cell & Developmental Biology
Journal title
CELLULAR AND MOLECULAR LIFE SCIENCES
ISSN journal
1420-682X → ACNP
Volume
58
Issue
1
Year of publication
2001
Pages
72 - 79
Database
ISI
SICI code
1420-682X(200101)58:1<72:PFMSIT>2.0.ZU;2-J
Abstract
Advances in methods of structure determination have led to the accumulation of large amounts of protein structural data. Some 500 distinct protein fol ds have now been characterized, representing one-third of all globular fold s that exist. The range of known structural types and the relatively large fraction of the protein universe that has already been sampled have greatly facilitated the discovery of some unifying principles governing protein st ructure and evolutionary relationships. These include a highly skewed distr ibution of topological arrangements of secondary-structure elements that fa vors a few very common connectivities and a highly skewed distribution in t he capacity of folds to accommodate unrelated sequences. These and other ob servations suggest that the number of folds is far fewer than the number of genes, and that the fold universe is dominated by a small number of giant attractors that accommodate large numbers of unrelated sequences. Thus all basic protein folds will likely be determined in the near future, laying th e foundation for a comprehensive understanding of the biochemical and cellu lar functions of whole organisms.