![]() | extracellular side |
| cytoplasmic side |
| 1gmi » C2 domain of protein kinase C epsilon | |
|---|---|
| Depth | 2.0 ± 1.1 Å |
| Tilt Angle | 41 ± 10° |
| ΔGtransfer | -5.1 kcal/mol |
| Links to 1gmi | PDB Sum, SCOP, MSD, OCA, MMDB, Dali |
| Topology | cytoplasmic |
| Resolution | 1.7 Å |
| Related PDB Sum entries | none |
| Number of subunits | 1 |
| Experimental Verification for 1gmi » C2 domain of protein kinase C epsilon |
|---|
| Residue I89 and partially V29 and P31 penetrate the bilayer core. According to muatgenesis studies, the most important residue for membrane binding is I89 (Corbalan-Garcia et al. 2003). The binding is also affected by replacing Y91 and in the triple mutant W23A/R26A/R32A. These residues are in the membrane interfacial region in the calculated orientation. |
| 1 reference |
|---|
| Corbalan-Garcia S, Sanchez-Carrillo S, Garcia-Garcia J, Gomez-Fernandez JC. 2003. Characterization of the membrane binding mode of the C2 domain of PKC epsilon. Biochemistry. 42:11661-8. PubMed |