1CDM

MODULATION OF CALMODULIN PLASTICITY IN MOLECULAR RECOGNITION ON THE BASIS OF X-RAY STRUCTURES

Summary for 1CDM

• Entry DOI: 10.2210/pdb1cdm/pdb
• Descriptor: PEPTIDE CALMODULIN-DEPENDENT PROTEIN KINASE II, CALMODULIN, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: calcium-binding protein
• Biological source: Bos taurus (cattle)
• Cellular location: Cytoplasm: P62157; Cell junction, synapse, presynaptic cell membrane: P11275
• Total number of polymer chains: 2
• Total formula weight: 19324.71

Authors

Meador, W.E.,Quiocho, F.A. (deposition date: 1993-10-08, release date: 1994-08-31, Last modification date: 2024-02-07)

Primary citation

Meador, W.E.,Means, A.R.,Quiocho, F.A.
Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structures.
Science, 262:1718-1721, 1993

PubMed Abstract: Calmodulin is the primary calcium-dependent signal transducer and regulator of a wide variety of essential cellular functions. The structure of calcium-calmodulin bound to the peptide corresponding to the calmodulin-binding domain of brain calmodulin-dependent protein kinase II alpha was determined to 2 angstrom resolution. A comparison to two other calcium-calmodulin structures reveals how the central helix unwinds in order to position the two domains optimally in the recognition of different target enzymes and clarifies the role of calcium in maintaining recognition-competent domain structures.

PubMed: 8259515

Experimental method

X-RAY DIFFRACTION (2 Å)