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

File:1cdm.gif


PDB ID 1cdm

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, resolution 2.0Å
Ligands:
Coordinates: save as pdb, mmCIF, xml



OverviewOverview

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.

About this StructureAbout this Structure

1CDM is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structures., Meador WE, Means AR, Quiocho FA, Science. 1993 Dec 10;262(5140):1718-21. PMID:8259515

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