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C2 domain
| C2 domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 The C2-domain of C.absonum α-toxin (PDB 1OLP). β-strands are shown in yellow, α-helices in red, loops in green. Co-ordinated calcium ions are in cyan. | |||||||||
| Identifiers | |||||||||
| Symbol | C2 | ||||||||
| Pfam | PF00168 | ||||||||
| Pfam clan | CL0154 | ||||||||
| ECOD | 11.2.1 | ||||||||
| InterPro | IPR000008 | ||||||||
| SMART | C2 | ||||||||
| PROSITE | PDOC00380 | ||||||||
| SCOP2 | 1qas / SCOPe / SUPFAM | ||||||||
| OPM superfamily | 45 | ||||||||
| OPM protein | 1ugk | ||||||||
| CDD | cd00030 | ||||||||
| |||||||||
| Phosphoinositide 3-kinase C2 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
 Structure of phosphoinositide 3-kinase.[1] | |||||||||||
| Identifiers | |||||||||||
| Symbol | PI3K_C2 | ||||||||||
| Pfam | PF00792 | ||||||||||
| Pfam clan | CL0154 | ||||||||||
| ECOD | 11.2.1 | ||||||||||
| InterPro | IPR002420 | ||||||||||
| SMART | PI3K_C2 | ||||||||||
| PROSITE | PDOC50004 | ||||||||||
| SCOP2 | 1e8x / SCOPe / SUPFAM | ||||||||||
| CDD | cd08380 | ||||||||||
| |||||||||||
A C2 domain is a protein structural domain involved in targeting proteins to cell membranes. The typical version (PKC-C2) has a beta-sandwich composed of 8 β-strands that co-ordinates two or three calcium ions, which bind in a cavity formed by the first and final loops of the domain, on the membrane binding face. Many other C2 domain families don't have calcium binding activity.[2][3]
- ^ Walker EH, Pacold ME, Perisic O, Stephens L, Hawkins PT, Wymann MP, Williams RL (October 2000). "Structural determinants of phosphoinositide 3-kinase inhibition by wortmannin, LY294002, quercetin, myricetin, and staurosporine". Molecular Cell. 6 (4): 909–19. doi:10.1016/S1097-2765(05)00089-4. PMID 11090628.
- ^ Zhang D, Aravind L (December 2010). "Identification of novel families and classification of the C2 domain superfamily elucidate the origin and evolution of membrane targeting activities in eukaryotes". Gene. 469 (1–2): 18–30. doi:10.1016/j.gene.2010.08.006. PMC 2965036. PMID 20713135.
- ^ Zhang D, Aravind L (October 2012). "Novel transglutaminase-like peptidase and C2 domains elucidate the structure, biogenesis and evolution of the ciliary compartment". Cell Cycle. 11 (20): 3861–75. doi:10.4161/cc.22068. PMC 3495828. PMID 22983010.
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