Evidence that the kinesin light chain domain contains tetratricopeptide repeat units

J Struct Biol. 2012 Mar;177(3):602-12. doi: 10.1016/j.jsb.2012.01.010. Epub 2012 Feb 4.

Abstract

Homology models were built for various length sequences of the kinesin-1 light chain (KLC) domain of Drosophila melanogaster and subjected to 200 ns of all-atom molecular dynamics. We also cloned, expressed and characterized these regions spectroscopically. Results confirm that KLC contains tetratricopeptide repeat units; a regular array of repeating 34-residue helix-loop-helix monomers. Experimental and computational evidence is provided confirming the stability and overall helicity of individual TPR repeats as well as individual TPR units incorporated into a multi-TPR structure.

Publication types

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

MeSH terms

  • Animals
  • Drosophila Proteins / chemistry*
  • Drosophila melanogaster
  • Kinesins / chemistry*
  • Models, Molecular
  • Oligopeptides / chemistry*
  • Protein Conformation

Substances

  • Drosophila Proteins
  • Oligopeptides
  • Kinesins