Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain

Academic Article

Abstract

  • Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of the CAP-Gly domain of Caenorhabditis elegans F53F4.3 protein, solved by single wavelength sulfur-anomalous phasing, revealed a novel protein fold containing three β-sheets. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove. Residues in the groove are highly conserved as measured from the information content of the aligned sequences. The C-terminal tail of another molecule in the crystal is bound in this groove.
  • Digital Object Identifier (doi)

    Author List

  • Li S; Finley J; Liu ZJ; Qiu SH; Chen H; Luan CH; Carson M; Tsao J; Johnson D; Lin G
  • Start Page

  • 48596
  • End Page

  • 48601
  • Volume

  • 277
  • Issue

  • 50