Format

Send to

Choose Destination
See comment in PubMed Commons below
J Biol Chem. 2002 Dec 13;277(50):48596-601. Epub 2002 Sep 7.

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

Author information

1
Southeast Collaboratory for Structural Genomics, University of Georgia, Athens 30602, USA.

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.

PMID:
12221106
DOI:
10.1074/jbc.M208512200
[Indexed for MEDLINE]
Free full text
PubMed Commons home

PubMed Commons

0 comments

    Supplemental Content

    Full text links

    Icon for HighWire
    Loading ...
    Support Center