1byy

From Proteopedia

(Difference between revisions)

Revision as of 10:42, 19 May 2021

SODIUM CHANNEL IIA INACTIVATION GATE

Structural highlights

1byy is a 1 chain structure with sequence from Buffalo rat. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SCN2A_RAT] Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Rohl CA, Boeckman FA, Baker C, Scheuer T, Catterall WA, Klevit RE. Solution structure of the sodium channel inactivation gate. Biochemistry. 1999 Jan 19;38(3):855-61. PMID:9893979 doi:http://dx.doi.org/10.1021/bi9823380

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1byy"

@@ Line 3: / Line 3: @@
 <StructureSection load='1byy' size='340' side='right'caption='[[1byy]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1byy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BYY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BYY FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1byy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BYY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BYY FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1byy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1byy OCA], [http://pdbe.org/1byy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1byy RCSB], [http://www.ebi.ac.uk/pdbsum/1byy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1byy ProSAT]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1byy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1byy OCA], [https://pdbe.org/1byy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1byy RCSB], [https://www.ebi.ac.uk/pdbsum/1byy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1byy ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SCN2A_RAT SCN2A_RAT]] Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient.
+[[https://www.uniprot.org/uniprot/SCN2A_RAT SCN2A_RAT]] Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 29: / Line 29: @@
 ==See Also==
-*[[Ion channels|Ion channels]]
+*[[Ion channels 3D structures|Ion channels 3D structures]]
 == References ==
 <references/>

1byy

From Proteopedia

Revision as of 10:42, 19 May 2021

SODIUM CHANNEL IIA INACTIVATION GATE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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