1A06

CALMODULIN-DEPENDENT PROTEIN KINASE FROM RAT

Summary for 1A06

• Entry DOI: 10.2210/pdb1a06/pdb
• Descriptor: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE (2 entities in total)
• Functional Keywords: kinase, signal transduction, calcium/calmodulin
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cytoplasm: Q63450
• Total number of polymer chains: 1
• Total formula weight: 37517.70

Authors

Kuriyan, J.,Goldberg, J. (deposition date: 1997-12-09, release date: 1998-04-08, Last modification date: 2024-02-07)

Primary citation

Goldberg, J.,Nairn, A.C.,Kuriyan, J.
Structural basis for the autoinhibition of calcium/calmodulin-dependent protein kinase I.
Cell(Cambridge,Mass.), 84:875-887, 1996

PubMed Abstract: The crystal structure of calcium/calmodulin-dependent protein kinase I has been determined in the autoinhibited form. The C-terminal regulatory region of the enzyme forms a helix-loop-helix segment that extends across the two domains of the catalytic core, making multiple inhibitory interactions. Elements of the first regulatory alpha helix and the loop interfere with the binding site for peptide substrates, while the loop and the second helix interact with the ATP-binding domain to induce conformational changes that obstruct the nucleotide binding pocket. One part of the calmodulin recognition element protrudes away from the catalytic domain and is potentially available for an initial interaction with calmodulin. The structure provides a view of an intact calmodulin target and suggests that substantial structural changes will accompany kinase activation by calmodulin binding to the regulatory region.

PubMed: 8601311
DOI: 10.1016/S0092-8674(00)81066-1

Experimental method

X-RAY DIFFRACTION (2.5 Å)