2f3y

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(New page: 200px<br /> <applet load="2f3y" size="450" color="white" frame="true" align="right" spinBox="true" caption="2f3y, resolution 1.450&Aring;" /> '''Calmodulin/IQ doma...)
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[[Image:2f3y.gif|left|200px]]<br /><applet load="2f3y" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="2f3y" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2f3y, resolution 1.450&Aring;" />
caption="2f3y, resolution 1.450&Aring;" />
'''Calmodulin/IQ domain complex'''<br />
'''Calmodulin/IQ domain complex'''<br />
==Overview==
==Overview==
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Ca2+-dependent inactivation (CDI) and facilitation (CDF) of the Ca(v)1.2, Ca2+ channel require calmodulin binding to a putative IQ motif in the, carboxy-terminal tail of the pore-forming subunit. We present the 1.45 A, crystal structure of Ca2+-calmodulin bound to a 21 residue peptide, corresponding to the IQ domain of Ca(v)1.2. This structure shows that, parallel binding of calmodulin to the IQ domain is governed by hydrophobic, interactions. Mutations of residues I1672 and Q1673 in the peptide to, alanines, which abolish CDI but not CDF in the channel, do not greatly, alter the structure. Both lobes of Ca2+-saturated CaM bind to the IQ, peptide but isoleucine 1672, thought to form an intramolecular interaction, that drives CDI, is buried. These findings suggest that this structure, could represent the conformation that calmodulin assumes in CDF.
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Ca2+-dependent inactivation (CDI) and facilitation (CDF) of the Ca(v)1.2 Ca2+ channel require calmodulin binding to a putative IQ motif in the carboxy-terminal tail of the pore-forming subunit. We present the 1.45 A crystal structure of Ca2+-calmodulin bound to a 21 residue peptide corresponding to the IQ domain of Ca(v)1.2. This structure shows that parallel binding of calmodulin to the IQ domain is governed by hydrophobic interactions. Mutations of residues I1672 and Q1673 in the peptide to alanines, which abolish CDI but not CDF in the channel, do not greatly alter the structure. Both lobes of Ca2+-saturated CaM bind to the IQ peptide but isoleucine 1672, thought to form an intramolecular interaction that drives CDI, is buried. These findings suggest that this structure could represent the conformation that calmodulin assumes in CDF.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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2F3Y is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2F3Y OCA].
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2F3Y is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F3Y OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Fallon, J.L.]]
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[[Category: Fallon, J L.]]
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[[Category: Quiocho, F.A.]]
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[[Category: Quiocho, F A.]]
[[Category: CA]]
[[Category: CA]]
[[Category: MG]]
[[Category: MG]]
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[[Category: calmodulin]]
[[Category: calmodulin]]
[[Category: calmodulin complex]]
[[Category: calmodulin complex]]
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[[Category: cav1.2]]
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[[Category: cav1 2]]
[[Category: iq domain]]
[[Category: iq domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:59:23 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:17:31 2008''

Revision as of 15:17, 21 February 2008

Image:2f3y.gif

2f3y, resolution 1.450Å

Drag the structure with the mouse to rotate

Calmodulin/IQ domain complex

Contents

Overview

Ca2+-dependent inactivation (CDI) and facilitation (CDF) of the Ca(v)1.2 Ca2+ channel require calmodulin binding to a putative IQ motif in the carboxy-terminal tail of the pore-forming subunit. We present the 1.45 A crystal structure of Ca2+-calmodulin bound to a 21 residue peptide corresponding to the IQ domain of Ca(v)1.2. This structure shows that parallel binding of calmodulin to the IQ domain is governed by hydrophobic interactions. Mutations of residues I1672 and Q1673 in the peptide to alanines, which abolish CDI but not CDF in the channel, do not greatly alter the structure. Both lobes of Ca2+-saturated CaM bind to the IQ peptide but isoleucine 1672, thought to form an intramolecular interaction that drives CDI, is buried. These findings suggest that this structure could represent the conformation that calmodulin assumes in CDF.

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], Timothy syndrome OMIM:[114205]

About this Structure

2F3Y is a Protein complex structure of sequences from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of calmodulin bound to the hydrophobic IQ domain of the cardiac Ca(v)1.2 calcium channel., Fallon JL, Halling DB, Hamilton SL, Quiocho FA, Structure. 2005 Dec;13(12):1881-6. PMID:16338416

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