1A25

C2 DOMAIN FROM PROTEIN KINASE C (BETA)

Summary for 1A25

• Entry DOI: 10.2210/pdb1a25/pdb
• Descriptor: PROTEIN KINASE C (BETA), CALCIUM ION, O-PHOSPHOETHANOLAMINE, ... (4 entities in total)
• Functional Keywords: calcium++/phospholipid binding protein, calcium-binding protein
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cytoplasm: P68403
• Total number of polymer chains: 2
• Total formula weight: 34175.78

Authors

Sutton, R.B.,Sprang, S.R. (deposition date: 1998-01-16, release date: 1998-05-06, Last modification date: 2024-05-22)

Primary citation

Sutton, R.B.,Sprang, S.R.
Structure of the protein kinase Cbeta phospholipid-binding C2 domain complexed with Ca2+.
Structure, 6:1395-1405, 1998

PubMed Abstract: Conventional isoforms (alpha, beta and gamma) of protein kinase C (PKC) are synergistically activated by phosphatidylserine and Ca2+; both bind to C2 domains located within the PKC amino-terminal regulatory regions. C2 domains contain a bipartite or tripartite Ca2+-binding site formed by opposing loops at one end of the protein. Neither the structural basis for cooperativity between phosphatidylserine and Ca2+, nor the binding site for phosphatidylserine are known.

PubMed: 9817842
DOI: 10.1016/S0969-2126(98)00139-7

Experimental method

X-RAY DIFFRACTION (2.7 Å)