1BDY
C2 DOMAIN FROM PROTEIN KINASE C DELTA
Summary for 1BDY
| Entry DOI | 10.2210/pdb1bdy/pdb |
| Descriptor | PROTEIN KINASE C (2 entities in total) |
| Functional Keywords | protein kinase c, c2 domain, calcium, calcium-binding, duplication, atp-binding, transferase |
| Biological source | Rattus norvegicus (Norway rat) |
| Cellular location | Cytoplasm: P09215 |
| Total number of polymer chains | 2 |
| Total formula weight | 28028.42 |
| Authors | Pappa, H.,Murray-Rust, J.,Dekker, L.V.,Parker, P.J.,Mcdonald, N.Q. (deposition date: 1998-05-11, release date: 1998-10-14, Last modification date: 2024-02-07) |
| Primary citation | Pappa, H.,Murray-Rust, J.,Dekker, L.V.,Parker, P.J.,McDonald, N.Q. Crystal structure of the C2 domain from protein kinase C-delta. Structure, 6:885-894, 1998 Cited by PubMed Abstract: The protein kinase C (PKC) family of lipid-dependent serine/theonine kinases plays a central role in many intracellular eukaryotic signalling events. Members of the novel (delta, epsilon, eta, theta) subclass of PKC isotypes lack the Ca2+ dependence of the conventional PKC isotypes and have an N-terminal C2 domain, originally defined as V0 (variable domain zero). Biochemical data suggest that this domain serves to translocate novel PKC family members to the plasma membrane and may influence binding of PKC activators. PubMed: 9687370DOI: 10.1016/S0969-2126(98)00090-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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