C-CAP/cofactor C-like domain <p>The C-CAP/cofactor C-like domain is present in several cytoskeleton-related proteins, which also contain a number of additional domains [<cite idref="PUB00026629"/>, <cite idref="PUB00039797"/>, <cite idref="PUB00043710"/>, <cite idref="PUB00043711"/>]:<ul> <li>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.</li><li>Vertebrate retinitis pigmentosa 2 (XRP2). In <taxon tax_id="9606">Homo sapiens</taxon> (Human), it is the protein responsible for X-linked forms of retinitis pigmentosa, a disease characterised by severe retinal degeneration.</li> <li>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.</li> </ul> </p><p>The cyclase-associated protein C-CAP/cofactor C-like domain binds G-actin and is responsible for oligomerisation of the entire CAP molecule [<cite idref="PUB00026629"/>], whereas the XRP2 C-CAP/cofactor C-like domain is required for binding of ADP ribosylation factor-like protein 3 (Arl3) [<cite idref="PUB00039797"/>].</p><p>The central core of the C-CAP/cofactor C-like domain is composed of six coils of right-handed parallel beta-helices, termed coils 1-6, which form an elliptical barrel with a tightly packed interior. Each beta-helical coil is composed of three relatively short beta-strands, designated a-c, separated by sharp turns. Flanking the central beta-helical core is an N-terminal beta-strand, beta0, that packs antiparallel to the core, and strand beta7 packs antiparallel to the core near the C-terminal end of the parallel beta-helix [<cite idref="PUB00026629"/>, <cite idref="PUB00039797"/>]. </p>