1j7o
From Proteopedia
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==Overview== | ==Overview== | ||
- | The solution structure of Ca(2+)-ligated calmodulin is determined from | + | The solution structure of Ca(2+)-ligated calmodulin is determined from residual dipolar couplings measured in a liquid crystalline medium and from a large number of heteronuclear J couplings for defining side chains. Although the C-terminal domain solution structure is similar to the X-ray crystal structure, the EF hands of the N-terminal domain are considerably less open. The substantial differences in interhelical angles correspond to negligible changes in short interproton distances and, therefore, cannot be identified by comparison of NOEs and X-ray data. NOE analysis, however, excludes a two-state equilibrium in which the closed apo conformation is partially populated in the Ca(2+)-ligated state. The difference between the crystal and solution structures of Ca(2+)-calmodulin indicates considerable backbone plasticity within the domains of calmodulin, which is key to their ability to bind a wide range of targets. In contrast, the vast majority of side chains making up the target binding surface are locked into the same chi(1) rotameric states as in complexes with target peptide. |
==Disease== | ==Disease== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bax, A.]] | [[Category: Bax, A.]] | ||
- | [[Category: Chou, J | + | [[Category: Chou, J J.]] |
- | [[Category: Klee, C | + | [[Category: Klee, C B.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: calcium binding]] | [[Category: calcium binding]] | ||
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[[Category: mini beta strand]] | [[Category: mini beta strand]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:19:33 2008'' |
Revision as of 11:19, 21 February 2008
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Solution structure of Calcium-calmodulin N-terminal domain
Contents |
Overview
The solution structure of Ca(2+)-ligated calmodulin is determined from residual dipolar couplings measured in a liquid crystalline medium and from a large number of heteronuclear J couplings for defining side chains. Although the C-terminal domain solution structure is similar to the X-ray crystal structure, the EF hands of the N-terminal domain are considerably less open. The substantial differences in interhelical angles correspond to negligible changes in short interproton distances and, therefore, cannot be identified by comparison of NOEs and X-ray data. NOE analysis, however, excludes a two-state equilibrium in which the closed apo conformation is partially populated in the Ca(2+)-ligated state. The difference between the crystal and solution structures of Ca(2+)-calmodulin indicates considerable backbone plasticity within the domains of calmodulin, which is key to their ability to bind a wide range of targets. In contrast, the vast majority of side chains making up the target binding surface are locked into the same chi(1) rotameric states as in complexes with target peptide.
Disease
Known diseases associated with this structure: Cavernous malformations of CNS and retina OMIM:[604214], Cerebral cavernous malformations-1 OMIM:[604214], Hyperkeratotic cutaneous capillary-venous malformations associated with cerebral capillary malformations OMIM:[604214], Leukemia, acute T-cell lymphoblastic OMIM:[603025], Leukemia, acute myeloid OMIM:[603025]
About this Structure
1J7O is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Solution structure of Ca(2+)-calmodulin reveals flexible hand-like properties of its domains., Chou JJ, Li S, Klee CB, Bax A, Nat Struct Biol. 2001 Nov;8(11):990-7. PMID:11685248
Page seeded by OCA on Thu Feb 21 13:19:33 2008
Categories: Homo sapiens | Single protein | Bax, A. | Chou, J J. | Klee, C B. | CA | Calcium binding | Ef hands | Helix bundle | Mini beta strand