Limitações estruturais e funcionais na evolução de famílias de proteínas

Review

Nature Reviews Molecular Cell Biology 10, 709-720 (October 2009) | doi:10.1038/nrm2762

Structural and functional constraints in the evolution of protein families

Catherine L. Worth 1,2, Sungsam Gong 1 & Tom L. Blundell 1 About the authors

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.

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Author affiliations

Biochemistry Department, University of Cambridge, Cambridge, CB2 1GA, UK.

Leibniz-Institut für Molekulare Pharmakologie, Campus Berlin-Buch, Berlin, 13125, Germany.

Correspondence to: Tom L. Blundell1 Email: tom@cryst.bioc.cam.ac.uk

Published online 16 September 2009