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1BDY

C2 DOMAIN FROM PROTEIN KINASE C DELTA

Summary for 1BDY
Entry DOI10.2210/pdb1bdy/pdb
DescriptorPROTEIN KINASE C (2 entities in total)
Functional Keywordsprotein kinase c, c2 domain, calcium, calcium-binding, duplication, atp-binding, transferase
Biological sourceRattus norvegicus (Norway rat)
Cellular locationCytoplasm: P09215
Total number of polymer chains2
Total formula weight28028.42
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 citationPappa, 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: 9687370
DOI: 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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