The solution structure of the pH-induced monomer of dynein light-chain LC8 from Drosophila

Protein Sci. 2004 Mar;13(3):727-34. doi: 10.1110/ps.03462204. Epub 2004 Feb 6.


The structure of Drosophila LC8 pH-induced monomer has been determined by NMR spectroscopy using the program AutoStructure. The structure at pH 3 and 30 degrees C is similar to the individual subunits of mammalian LC8 dimer with the exception that a beta strand, which crosses between monomers to form an intersubunit beta-sheet in the dimer, is a flexible loop with turnlike conformations in the monomer. Increased flexibility in the interface region relative to the rest of the protein is confirmed by dynamic measurements based on (15)N relaxation. Comparison of the monomer and dimer structures indicates that LC8 is not a domain swapped dimer.

MeSH terms

  • Animals
  • Carrier Proteins / chemistry*
  • Carrier Proteins / genetics
  • Drosophila / chemistry
  • Drosophila Proteins / chemistry*
  • Drosophila Proteins / genetics
  • Dyneins
  • Hydrogen-Ion Concentration
  • Isotope Labeling
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Conformation
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Protein Subunits / chemistry*
  • Protein Subunits / genetics
  • Recombinant Proteins / chemistry
  • Structural Homology, Protein


  • Carrier Proteins
  • Drosophila Proteins
  • Protein Subunits
  • Recombinant Proteins
  • ctp protein, Drosophila
  • Dyneins