Structural and functional constraints in the evolution of protein families

Nat Rev Mol Cell Biol. 2009 Oct;10(10):709-20. doi: 10.1038/nrm2762. Epub 2009 Sep 16.

Abstract

High-throughput genomic sequencing has focused attention on understanding differences between species and between individuals. When this genetic variation affects protein sequences, the rate of amino acid substitution reflects both Darwinian selection for functionally advantageous mutations and selectively neutral evolution operating within the constraints of structure and function. During neutral evolution, whereby mutations accumulate by random drift, amino acid substitutions are constrained by factors such as the formation of intramolecular and intermolecular interactions and the accessibility to water or lipids surrounding the protein. These constraints arise from the need to conserve a specific architecture and to retain interactions that mediate functions in protein families and superfamilies.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution
  • Evolution, Molecular*
  • Hydrogen Bonding
  • Hydrophobic and Hydrophilic Interactions
  • Kinetics
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding
  • Protein Folding
  • Protein Structure, Secondary
  • Proteins / chemistry*
  • Proteins / metabolism*
  • Sequence Homology, Amino Acid

Substances

  • Proteins

Associated data

  • PDB/1GK8
  • PDB/1M2Z
  • PDB/1TME
  • PDB/2FGF
  • PDB/2OHXA
  • PDB/3APP
  • PDB/5PAL