Protein repeats: structures, functions, and evolution

M A Andrade, C Perez-Iratxeta, C P Ponting

Research output: Contribution to journalArticlepeer-review


Internal repetition within proteins has been a successful strategem on multiple separate occasions throughout evolution. Such protein repeats possess regular secondary structures and form multirepeat assemblies in three dimensions of diverse sizes and functions. In general, however, internal repetition affords a protein enhanced evolutionary prospects due to an enlargement of its available binding surface area. Constraints on sequence conservation appear to be relatively lax, due to binding functions ensuing from multiple, rather than, single repeats. Considerable sequence divergence as well as the short lengths of sequence repeats mean that repeat detection can be a particularly arduous task. We also consider the conundrum of how multiple repeats, which show strong structural and functional interdependencies, ever evolved from a single repeat ancestor. In this review, we illustrate each of these points by referring to six prolific repeat types (repeats in beta-propellers and beta-trefoils and tetratricopeptide, ankyrin, armadillo/HEAT, and leucine-rich repeats) and in other less-prolific but nonetheless interesting repeats.

Original languageEnglish
Pages (from-to)117-31
Number of pages15
JournalJournal of Structural Biology
Issue number2-3
Publication statusPublished - 12 Sep 2001


  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Evolution, Molecular
  • Humans
  • Molecular Sequence Data
  • Protein Structure, Secondary
  • Proteins
  • Repetitive Sequences, Amino Acid


Dive into the research topics of 'Protein repeats: structures, functions, and evolution'. Together they form a unique fingerprint.

Cite this