1f70: Difference between revisions
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[[Image:1f70.jpg|left|200px]] | [[Image:1f70.jpg|left|200px]] | ||
'''REFINED SOLUTION STRUCTURE OF CALMODULIN N-TERMINAL DOMAIN''' | {{Structure | ||
|PDB= 1f70 |SIZE=350|CAPTION= <scene name='initialview01'>1f70</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''REFINED SOLUTION STRUCTURE OF CALMODULIN N-TERMINAL DOMAIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1F70 is a [ | 1F70 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F70 OCA]. | ||
==Reference== | ==Reference== | ||
Study of conformational rearrangement and refinement of structural homology models by the use of heteronuclear dipolar couplings., Chou JJ, Li S, Bax A, J Biomol NMR. 2000 Nov;18(3):217-27. PMID:[http:// | Study of conformational rearrangement and refinement of structural homology models by the use of heteronuclear dipolar couplings., Chou JJ, Li S, Bax A, J Biomol NMR. 2000 Nov;18(3):217-27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11142512 11142512] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Xenopus laevis]] | [[Category: Xenopus laevis]] | ||
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[[Category: Li, S.]] | [[Category: Li, S.]] | ||
[[Category: calcium binding]] | [[Category: calcium binding]] | ||
[[Category: ef | [[Category: ef hand]] | ||
[[Category: four-helix bundle]] | [[Category: four-helix bundle]] | ||
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Revision as of 12:05, 20 March 2008
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REFINED SOLUTION STRUCTURE OF CALMODULIN N-TERMINAL DOMAIN
OverviewOverview
For an increasing fraction of proteins whose structures are being studied, sequence homology to known structures permits building of low resolution structural models. It is demonstrated that dipolar couplings, measured in a liquid crystalline medium, not only can validate such structural models, but also refine them. Here, experimental 1H-15N, 1Halpha-13Calpha, and 13C'-13Calpha dipolar couplings are shown to decrease the backbone rmsd between various homology models of calmodulin (CaM) and its crystal structure. Starting from a model of the Ca2+-saturated C-terminal domain of CaM, built from the structure of Ca2+-free recoverin on the basis of remote sequence homology, dipolar couplings are used to decrease the rmsd between the model and the crystal structure from 5.0 to 1.25 A. A better starting model, built from the crystal structure of Ca2+-saturated parvalbumin, decreases in rmsd from 1.25 to 0.93 A. Similarly, starting from the structure of the Ca2+-ligated CaM N-terminal domain, experimental dipolar couplings measured for the Ca2+-free form decrease the backbone rmsd relative to the refined solution structure of apo-CaM from 4.2 to 1.0 A.
About this StructureAbout this Structure
1F70 is a Single protein structure of sequence from Xenopus laevis. Full crystallographic information is available from OCA.
ReferenceReference
Study of conformational rearrangement and refinement of structural homology models by the use of heteronuclear dipolar couplings., Chou JJ, Li S, Bax A, J Biomol NMR. 2000 Nov;18(3):217-27. PMID:11142512
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