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

Songlin Li, Jim Finley, Zhi Jie Liu, Shi Hong Qiu, Hongli Chen, Chi Hao Luan, Mike Carson, Jun Tsao, David Johnson, Guangda Lin, Jun Zhao, Willie Thomas, Lisa A. Nagy, Bingdong Sha, Lawrence J. DeLucas, Bi Cheng Wang, Ming Luo*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

85 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)48596-48601
Number of pages6
JournalJournal of Biological Chemistry
Issue number50
StatePublished - Dec 13 2002

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain'. Together they form a unique fingerprint.

Cite this