Protein homorepeats sequences, structures, evolution, and functions.
The vast majority of protein sequences are aperiodic; they do not have any strong bias in the amino acid composition, and they use a subtle mixture of all or most of the 20 amino acid residues to code a great number of various structures and functions. In this context, homorepeats, runs of a single amino acid residue, represent unusual, eye-catching motifs in proteins. Despite the sequence simplicity and relatively small size, the homorepeat runs have a strong potential for molecular interactions due to the excessively high local concentration of a certain physico-chemical property. Appearance of such runs within proteins may give them new structural and functional features. An increasing number of studies demonstrate the abundance of these motifs in proteins, their important roles in biological processes, and their link to a number of hereditary and age-related diseases. In this chapter, we summarize data on the distribution of homorepeats in proteomes and on their structural properties, evolution, and functions.
Jorda
Julien
J
Centre de Recherches de Biochimie Macromoléculaire UMR 5237, CNRS, University of Montpellier 1 and 2, Montpellier, France.
Kajava
Andrey V
AV
D000595:Amino Acid Sequence; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000502:physiology*; D020543:Proteome; D020539:Sequence Analysis, Protein
D011506:Proteins; D020543:Proteome