1cdm
From Proteopedia
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[[Image:1cdm.gif|left|200px]] | [[Image:1cdm.gif|left|200px]] | ||
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'''MODULATION OF CALMODULIN PLASTICITY IN MOLECULAR RECOGNITION ON THE BASIS OF X-RAY STRUCTURES''' | '''MODULATION OF CALMODULIN PLASTICITY IN MOLECULAR RECOGNITION ON THE BASIS OF X-RAY STRUCTURES''' | ||
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[[Category: Meador, W E.]] | [[Category: Meador, W E.]] | ||
[[Category: Quiocho, F A.]] | [[Category: Quiocho, F A.]] | ||
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- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:36:46 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 09:36, 2 May 2008
MODULATION OF CALMODULIN PLASTICITY IN MOLECULAR RECOGNITION ON THE BASIS OF X-RAY STRUCTURES
Overview
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 Structure
1CDM is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.
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:8259515 Page seeded by OCA on Fri May 2 12:36:46 2008