Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC51329C-CAP/cofactor C-like domain profile
View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC51329
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) (see <PDOC00835>), 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 localization and the establishment of cell polarity.
- Vertebrate retinitis pigmentosa 2 (XRP2). In human, the protein responsible for X-linked forms of retinitis pigmentosa, a disease characterized 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 α- and β-tubulin heterodimer.
The cyclase-associated protein C-CAP/cofactor C-like domain binds G-actin and is responsible for oligomerization 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-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. | |
| Source | Biochemistry 43:10628-10641(2004). | |
| PubMed ID | 15311924 | |
| DOI | 10.1021/bi049071r |
| 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. | |
| Source | Structure 14:367-378(2006). | |
| PubMed ID | 16472755 | |
| DOI | 10.1016/j.str.2005.11.008 |
| 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. | |
| Source | Traffic 0:0-0(2007). | |
| PubMed ID | 17645436 | |
| DOI | 10.1111/j.1600-0854.2007.00611.x |
| 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). | |
| PubMed ID | 14536023 | |
| DOI | 10.1186/1471-2105-4-46 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.