Segmented alpha-helical coiled-coil structure of the protein giardin from the Giardia cytoskeleton

J Mol Biol. 1988 Dec 5;204(3):789-95. doi: 10.1016/0022-2836(88)90370-1.


The parasitic flagellate Giardia is the source of a filamentous protein, giardin, which binds to microtubules. The primary sequence of one giardin chain has been decoded from the base sequences of cDNAs isolated by antibody screens of a library constructed in the expression vector lambda gt11. The amino acid sequence favours a continuous alpha-helical fold for the protein without any inserts of a non-helical character. Analysis of apolar residue positions revealed 35 repeating heptads consistent with coiled-coil structure. This conformation relates giardin to the alpha-type fibrous proteins (k-m-e-f class) like tropomyosin and myosin (also found in Giardia). The giardin sequence has a regular series of skip residues like those at certain positions in the rod section of nematode myosin where the internal apolar seam of the coiled coil is shifted on the helix surface. The skips divide the giardin coil into quasi-equivalent structural segments about 4 nm in length, which might be domains for combining with tubulin subunits in the microtubule surface lattice.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cytoskeletal Proteins*
  • Giardia / metabolism*
  • Microtubules / metabolism
  • Molecular Sequence Data
  • Protein Conformation
  • Protozoan Proteins*


  • Cytoskeletal Proteins
  • Protozoan Proteins
  • giardin protein, Giardia lamblia