2bcx

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(New page: 200px<br /><applet load="2bcx" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bcx, resolution 2.000&Aring;" /> '''Crystal structure o...)
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[[Image:2bcx.jpg|left|200px]]<br /><applet load="2bcx" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2bcx.jpg|left|200px]]<br /><applet load="2bcx" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2bcx, resolution 2.000&Aring;" />
caption="2bcx, resolution 2.000&Aring;" />
'''Crystal structure of calmodulin in complex with a ryanodine receptor peptide'''<br />
'''Crystal structure of calmodulin in complex with a ryanodine receptor peptide'''<br />
==Overview==
==Overview==
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Calmodulin regulates ryanodine receptor-mediated Ca(2+) release through a, conserved binding site. The crystal structure of Ca(2+)-calmodulin bound, to this conserved site reveals that calmodulin recognizes two hydrophobic, anchor residues at a novel "1-17" spacing that brings the calmodulin lobes, close together but prevents them from contacting one another. NMR residual, dipolar couplings demonstrate that the detailed structure of each lobe is, preserved in solution but also show that the lobes experience domain, motions within the complex. FRET measurements confirm the close approach, of the lobes in binding the 1-17 target and show that calmodulin binds, with one lobe to a peptide lacking the second anchor. We suggest that, calmodulin regulates the Ca(2+) channel by switching between the, contiguous binding mode seen in our crystal structure and a state where, one lobe of calmodulin contacts the conserved binding site while the other, interacts with a noncontiguous site on the channel.
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Calmodulin regulates ryanodine receptor-mediated Ca(2+) release through a conserved binding site. The crystal structure of Ca(2+)-calmodulin bound to this conserved site reveals that calmodulin recognizes two hydrophobic anchor residues at a novel "1-17" spacing that brings the calmodulin lobes close together but prevents them from contacting one another. NMR residual dipolar couplings demonstrate that the detailed structure of each lobe is preserved in solution but also show that the lobes experience domain motions within the complex. FRET measurements confirm the close approach of the lobes in binding the 1-17 target and show that calmodulin binds with one lobe to a peptide lacking the second anchor. We suggest that calmodulin regulates the Ca(2+) channel by switching between the contiguous binding mode seen in our crystal structure and a state where one lobe of calmodulin contacts the conserved binding site while the other interacts with a noncontiguous site on the channel.
==About this Structure==
==About this Structure==
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2BCX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BCX OCA].
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2BCX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BCX OCA].
==Reference==
==Reference==
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: MacKenzie, K.R.]]
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[[Category: MacKenzie, K R.]]
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[[Category: Maximciuc, A.A.]]
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[[Category: Maximciuc, A A.]]
[[Category: Shamoo, Y.]]
[[Category: Shamoo, Y.]]
[[Category: CA]]
[[Category: CA]]
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[[Category: type-2 turn]]
[[Category: type-2 turn]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:44:06 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:36:27 2008''

Revision as of 14:36, 21 February 2008


2bcx, resolution 2.000Å

Drag the structure with the mouse to rotate

Crystal structure of calmodulin in complex with a ryanodine receptor peptide

Overview

Calmodulin regulates ryanodine receptor-mediated Ca(2+) release through a conserved binding site. The crystal structure of Ca(2+)-calmodulin bound to this conserved site reveals that calmodulin recognizes two hydrophobic anchor residues at a novel "1-17" spacing that brings the calmodulin lobes close together but prevents them from contacting one another. NMR residual dipolar couplings demonstrate that the detailed structure of each lobe is preserved in solution but also show that the lobes experience domain motions within the complex. FRET measurements confirm the close approach of the lobes in binding the 1-17 target and show that calmodulin binds with one lobe to a peptide lacking the second anchor. We suggest that calmodulin regulates the Ca(2+) channel by switching between the contiguous binding mode seen in our crystal structure and a state where one lobe of calmodulin contacts the conserved binding site while the other interacts with a noncontiguous site on the channel.

About this Structure

2BCX is a Protein complex structure of sequences from Gallus gallus with as ligand. Full crystallographic information is available from OCA.

Reference

Complex of calmodulin with a ryanodine receptor target reveals a novel, flexible binding mode., Maximciuc AA, Putkey JA, Shamoo Y, Mackenzie KR, Structure. 2006 Oct;14(10):1547-56. PMID:17027503

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