1cdm: Difference between revisions
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[[Image:1cdm.gif|left|200px]] | [[Image:1cdm.gif|left|200px]] | ||
'''MODULATION OF CALMODULIN PLASTICITY IN MOLECULAR RECOGNITION ON THE BASIS OF X-RAY STRUCTURES''' | {{Structure | ||
|PDB= 1cdm |SIZE=350|CAPTION= <scene name='initialview01'>1cdm</scene>, resolution 2.0Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''MODULATION OF CALMODULIN PLASTICITY IN MOLECULAR RECOGNITION ON THE BASIS OF X-RAY STRUCTURES''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1CDM is a [ | 1CDM is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CDM OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8259515 8259515] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: calcium-binding protein]] | [[Category: calcium-binding protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:22:59 2008'' |
Revision as of 11:23, 20 March 2008
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Coordinates: | save as pdb, mmCIF, xml |
MODULATION OF CALMODULIN PLASTICITY IN MOLECULAR RECOGNITION ON THE BASIS OF X-RAY STRUCTURES
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
Page seeded by OCA on Thu Mar 20 10:22:59 2008