Fold change in evolution of protein structures

Research output: Contribution to journalArticle

327 Scopus citations

Abstract

Typically, protein spatial structures are more conserved in evolution than amino acid sequences. However, the recent explosion of sequence and structure information accompanied by the development of powerful computational methods led to the accumulation of examples of homologous proteins with globally distinct structures. Significant sequence conservation, local structural resemblance, and functional similarity strongly indicate evolutionary relationships between these proteins despite pronounced structural differences at the fold level. Several mechanisms such as insertions/deletions/substitutions, circular permutations, and rearrangements in β-sheet topologies account for the majority of detected structural irregularities. The existence of evolutionarily related proteins that possess different folds brings new challenges to the homology modeling techniques and the structure classification strategies and offers new opportunities for protein design in experimental studies.

Original languageEnglish (US)
Pages (from-to)167-185
Number of pages19
JournalJournal of Structural Biology
Volume134
Issue number2-3
DOIs
StatePublished - Jan 1 2001

Keywords

  • Circular permutation
  • Conformational change
  • Deletion
  • Homology modeling
  • Insertion
  • Molecular evolution
  • Protein structure classification

ASJC Scopus subject areas

  • Structural Biology

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