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PDBsum entry 3wfn
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Metal binding protein
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PDB id
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3wfn
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Contents |
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169 a.a.
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138 a.a.
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166 a.a.
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PDB id:
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| Name: |
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Metal binding protein
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Title:
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Crystal structure of nav1.6 iq motif in complex with apo-cam
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Structure:
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Calmodulin, sodium channel protein type 8 subunit alpha. Chain: b, c, d, e. Synonym: cam, sodium channel protein type viii subunit alpha, voltage-gated sodium channel subunit alpha nav1.6. Engineered: yes. Other_details: chimera protein of calmodulin (uniprot p62204 calm_mouse) and nav1.6 iq motif from sodium channel protein type 8 subunit alpha (uniprot q9wtu3 scn8a_mouse, residues 1893-1914)
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Source:
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Mus musculus. Mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.95Å
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R-factor:
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0.201
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R-free:
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0.237
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Authors:
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V.P.R.Chichili,J.Sivaraman
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Key ref:
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V.P.Reddy Chichili
et al.
(2013).
Structural basis for the modulation of the neuronal voltage-gated sodium channel NaV1.6 by calmodulin.
Sci Rep,
3,
2435.
PubMed id:
DOI:
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Date:
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23-Jul-13
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Release date:
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28-Aug-13
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PROCHECK
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Headers
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References
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P0DP26
(CALM1_MOUSE) -
Calmodulin-1 from Mus musculus
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Seq:
Struc:
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149 a.a.
169 a.a.*
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Q9WTU3
(SCN8A_MOUSE) -
Sodium channel protein type 8 subunit alpha from Mus musculus
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Seq:
Struc:
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1978 a.a.
169 a.a.*
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P0DP26
(CALM1_MOUSE) -
Calmodulin-1 from Mus musculus
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Seq:
Struc:
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149 a.a.
138 a.a.*
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Q9WTU3
(SCN8A_MOUSE) -
Sodium channel protein type 8 subunit alpha from Mus musculus
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Seq:
Struc:
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1978 a.a.
138 a.a.*
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DOI no:
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Sci Rep
3:2435
(2013)
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PubMed id:
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Structural basis for the modulation of the neuronal voltage-gated sodium channel NaV1.6 by calmodulin.
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V.P.Reddy Chichili,
Y.Xiao,
J.Seetharaman,
T.R.Cummins,
J.Sivaraman.
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ABSTRACT
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The neuronal-voltage gated sodium channel (VGSC), NaV1.6, plays an important
role in propagating action potentials along myelinated axons. Calmodulin (CaM)
is known to modulate the inactivation kinetics of NaV1.6 by interacting with its
IQ motif. Here we report the crystal structure of apo-CaM:NaV1.6IQ motif, along
with functional studies. The IQ motif of NaV1.6 adopts an α-helical
conformation in its interaction with the C-lobe of CaM. CaM uses different
residues to interact with NaV1.6IQ motif depending on the presence or absence of
Ca(2+). Three residues from NaV1.6, Arg1902, Tyr1904 and Arg1905 were identified
as the key common interacting residues in both the presence and absence of
Ca(2+). Substitution of Arg1902 and Tyr1904 with alanine showed a reduced rate
of NaV1.6 inactivation in electrophysiological experiments in vivo. Compared
with other CaM:NaV complexes, our results reveal a different mode of interaction
for CaM:NaV1.6 and provides structural insight into the isoform-specific
modulation of VGSCs.
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