|PROSITE documentation PDOC51329 [for PROSITE entry PS51329]|
The cyclase-associated protein C-CAP/cofactor C-like domain binds G-actin and is responsible for oligomerization of the entire CAP molecule , whereas the XRP2 C-CAP/cofactor C-like domain is required for binding of ADP ribosylation factor-like protein 3 (Arl3) .
The central core of the C-CAP/cofactor C-like domain is composed of six coils of right-handed parallel β-helix, termed coils 1-6, which form an elliptical barrel with a tightly packed interior. Each β-helical coil is composed of three relatively short β-strands, designated a-c, separated by sharp turns. Flanking the central β-helical core is an N-terminal β-strand, β0, that packs antiparallel to the core, and strand β7 packs antiparallel to the core near the C-terminal end of the parallel β-helix (see <PDB:1K4Z>) [1,2].
The profile we developed covers the C-CAP/cofactor C-like domain.Last update:
August 2007 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Dodatko T., Fedorov A.A., Grynberg M., Patskovsky Y., Rozwarski D.A., Jaroszewski L., Aronoff-Spencer E., Kondraskina E., Irving T., Godzik A., Almo S.C.|
|Title||Crystal structure of the actin binding domain of the cyclase-associated protein.|
|2||Authors||Kuehnel K., Veltel S., Schlichting I., Wittinghofer A.|
|Title||Crystal structure of the human retinitis pigmentosa 2 protein and its interaction with Arl3.|
|3||Authors||Stephan A., Vaughan S., Shaw M.K., Gull K., McKean P.G.|
|Title||An Essential Quality Control Mechanism at the Eukaryotic Basal Body Prior to Intraflagellar Transport.|
|4||Authors||Grynberg M., Jaroszewski L., Godzik A.|
|Title||Domain analysis of the tubulin cofactor system: a model for tubulin folding and dimerization.|
|Source||BMC Bioinformatics 4:46-46(2003).|