Download MendeleyCrystal Structure of the Cytoskeleton-associated Protein Glycine-rich (CAP-Gly) Domain
Li, S., Finley, J., Liu, Z.-J., Qiu, S.H., Luan, C.H., Carson, M., Tsao, J., Johnson, D., Lin, G., Zhao, J., Thomas, W., Nagy, L.A., Sha, B., DeLucas, L.J., Wang, B.-C., Luo, M.(2002) J Biol Chem 277: 48596-48601
- PubMed: 12221106
- DOI: https://doi.org/10.1074/jbc.M208512200
- Primary Citation of Related Structures:
1LPL, 1TOV - PubMed 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 beta-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.
Organizational Affiliation:
Southeast Collaboratory for Structural Genomics, University of Georgia, Athens 30602, USA.
