D
IPR017901

C-CAP/cofactor C-like domain

InterPro entry
Short nameC-CAP_CF_C-like
Overlapping
homologous
superfamilies
 
domain relationships

Description

The C-CAP/cofactor C-like domain is present in several cytoskeleton-related proteins, which also contain a number of additional domains
[1, 2, 3, 4]
:


 * Eukaryotic cyclase-associated protein (CAP or SRV2), a modular actin monomer binding that directly regulates filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localisation and the establishment of cell polarity.
 * Vertebrate retinitis pigmentosa 2 (XRP2). In Homo sapiens (Human), it is the protein responsible for X-linked forms of retinitis pigmentosa, a disease characterised by severe retinal degeneration.
 * Eukaryotic tubulin-specific chaperone cofactor C (TBCC), a GTPase- activating component of the tubulin-folding supercomplex, which directs the assembly of the alpha- and beta-tubulin heterodimer.


The cyclase-associated protein C-CAP/cofactor C-like domain binds G-actin and is responsible for oligomerisation of the entire CAP molecule
[1]
, whereas the XRP2 C-CAP/cofactor C-like domain is required for binding of ADP ribosylation factor-like protein 3 (Arl3)
[2]
.

The central core of the C-CAP/cofactor C-like domain is composed of six coils of right-handed parallel β-helices, 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
[1, 2]
.

References

1.Crystal structure of the actin binding domain of the cyclase-associated protein. Dodatko T, Fedorov AA, Grynberg M, Patskovsky Y, Rozwarski DA, Jaroszewski L, Aronoff-Spencer E, Kondraskina E, Irving T, Godzik A, Almo SC. Biochemistry 43, 10628-41, (2004). View articlePMID: 15311924

2.Crystal structure of the human retinitis pigmentosa 2 protein and its interaction with Arl3. Kuhnel K, Veltel S, Schlichting I, Wittinghofer A. Structure 14, 367-78, (2006). View articlePMID: 16472755

3.An essential quality control mechanism at the eukaryotic basal body prior to intraflagellar transport. Stephan A, Vaughan S, Shaw MK, Gull K, McKean PG. Traffic 8, 1323-30, (2007). View articlePMID: 17645436

4.Domain analysis of the tubulin cofactor system: a model for tubulin folding and dimerization. Grynberg M, Jaroszewski L, Godzik A. BMC Bioinformatics 4, 46, (2003). View articlePMID: 14536023

Contributing Member Database Entry
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.