5W4S
Solution structure of C2 domain from protein kinase C alpha in ternary complex with calcium and V5-pHM peptide
Summary for 5W4S
| Entry DOI | 10.2210/pdb5w4s/pdb |
| Related | 2nce |
| NMR Information | BMRB: 30305 |
| Descriptor | Protein kinase C alpha type, V5-pHM peptide, CALCIUM ION (3 entities in total) |
| Functional Keywords | transferase, phosphorylation |
| Biological source | Rattus norvegicus (Rat) More |
| Total number of polymer chains | 2 |
| Total formula weight | 17618.79 |
| Authors | Yang, Y.,Igumenova, T.I. (deposition date: 2017-06-12, release date: 2018-04-25, Last modification date: 2024-10-30) |
| Primary citation | Yang, Y.,Shu, C.,Li, P.,Igumenova, T.I. Structural Basis of Protein Kinase C alpha Regulation by the C-Terminal Tail. Biophys. J., 114:1590-1603, 2018 Cited by PubMed Abstract: Protein kinase C (PKC) isoenzymes are multi-modular proteins activated at the membrane surface to regulate signal transduction processes. When activated by second messengers, PKC undergoes a drastic conformational and spatial transition from the inactive cytosolic state to the activated membrane-bound state. The complete structure of either state of PKC remains elusive. We demonstrate, using NMR spectroscopy, that the isolated Ca-sensing membrane-binding C2 domain of the conventional PKCα interacts with a conserved hydrophobic motif of the kinase C-terminal region, and we report a structural model of the complex. Our data suggest that the C-terminal region plays a dual role in regulating the PKC activity: activating, through sensitization of PKC to intracellular Ca oscillations; and auto-inhibitory, through its interaction with a conserved positively charged region of the C2 domain. PubMed: 29642029DOI: 10.1016/j.bpj.2017.12.030 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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