1byy

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(New page: 200px<br /><applet load="1byy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1byy" /> '''SODIUM CHANNEL IIA INACTIVATION GATE'''<br /...)
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[[Image:1byy.gif|left|200px]]<br /><applet load="1byy" size="350" color="white" frame="true" align="right" spinBox="true"
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'''SODIUM CHANNEL IIA INACTIVATION GATE'''<br />
'''SODIUM CHANNEL IIA INACTIVATION GATE'''<br />
==Overview==
==Overview==
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The sodium channel initiates action potentials by opening in response to, membrane depolarization. Fast channel inactivation, which is required for, proper physiological function, is mediated by a cytoplasmic loop proposed, to occlude the ion pore via a hinged lid mechanism with the triad IFM, serving as a hydrophobic "latch". The NMR solution structure of the, isolated inactivation gate reveals a stably folded core comprised of an, alpha-helix capped by an N-terminal turn, supporting a model in which the, tightly folded core containing the latch motif pivots on a more flexible, hinge region to occlude the pore during inactivation. The structure, in, combination with substituted cysteine mutagenesis experiments, indicates, that the IFM triad and adjacent Thr are essential components of the latch, and suggests differing roles for the residues of the IFMT motif in fast, inactivation.
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The sodium channel initiates action potentials by opening in response to membrane depolarization. Fast channel inactivation, which is required for proper physiological function, is mediated by a cytoplasmic loop proposed to occlude the ion pore via a hinged lid mechanism with the triad IFM serving as a hydrophobic "latch". The NMR solution structure of the isolated inactivation gate reveals a stably folded core comprised of an alpha-helix capped by an N-terminal turn, supporting a model in which the tightly folded core containing the latch motif pivots on a more flexible hinge region to occlude the pore during inactivation. The structure, in combination with substituted cysteine mutagenesis experiments, indicates that the IFM triad and adjacent Thr are essential components of the latch and suggests differing roles for the residues of the IFMT motif in fast inactivation.
==About this Structure==
==About this Structure==
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1BYY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BYY OCA].
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1BYY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BYY OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Baker, C.]]
[[Category: Baker, C.]]
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[[Category: Boeckman, F.A.]]
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[[Category: Boeckman, F A.]]
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[[Category: Catterall, W.A.]]
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[[Category: Catterall, W A.]]
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[[Category: Klevit, R.E.]]
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[[Category: Klevit, R E.]]
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[[Category: Rohl, C.A.]]
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[[Category: Rohl, C A.]]
[[Category: Scheuer, T.]]
[[Category: Scheuer, T.]]
[[Category: sodium channel]]
[[Category: sodium channel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:02:10 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:00:37 2008''

Revision as of 10:00, 21 February 2008


1byy

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SODIUM CHANNEL IIA INACTIVATION GATE

Overview

The sodium channel initiates action potentials by opening in response to membrane depolarization. Fast channel inactivation, which is required for proper physiological function, is mediated by a cytoplasmic loop proposed to occlude the ion pore via a hinged lid mechanism with the triad IFM serving as a hydrophobic "latch". The NMR solution structure of the isolated inactivation gate reveals a stably folded core comprised of an alpha-helix capped by an N-terminal turn, supporting a model in which the tightly folded core containing the latch motif pivots on a more flexible hinge region to occlude the pore during inactivation. The structure, in combination with substituted cysteine mutagenesis experiments, indicates that the IFM triad and adjacent Thr are essential components of the latch and suggests differing roles for the residues of the IFMT motif in fast inactivation.

About this Structure

1BYY is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Solution structure of the sodium channel inactivation gate., Rohl CA, Boeckman FA, Baker C, Scheuer T, Catterall WA, Klevit RE, Biochemistry. 1999 Jan 19;38(3):855-61. PMID:9893979

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