Structural drift: a possible path to protein fold change

Bioinformatics. 2005 Apr 15;21(8):1308-10. doi: 10.1093/bioinformatics/bti227. Epub 2004 Dec 16.

Abstract

Summary: Along with their mutating sequences, protein structures change in time. Analyzing a formate dehydrogenase domain that is evolutionarily related to ferredoxin, but simultaneously contains all the structural elements of a beta-Grasp fold, we illustrate here a mechanism termed as structural drift, by which changes to a protein fold can occur.

Contact: grishin@chop.swmed.edu.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Carrier Proteins / chemistry
  • Carrier Proteins / genetics
  • Evolution, Molecular*
  • Ferredoxins / chemistry*
  • Ferredoxins / genetics*
  • Formate Dehydrogenases / chemistry*
  • Formate Dehydrogenases / genetics*
  • Genetic Drift*
  • Membrane Proteins
  • Models, Chemical*
  • Models, Molecular*
  • Protein Folding
  • Protein Structure, Tertiary
  • Protein Subunits
  • Sequence Analysis, Protein / methods*
  • Structure-Activity Relationship

Substances

  • Carrier Proteins
  • Ferredoxins
  • GRASP protein, human
  • Membrane Proteins
  • Protein Subunits
  • Formate Dehydrogenases