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1ors

From Proteopedia

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Current revision

X-ray structure of the KvAP potassium channel voltage sensor in complex with an Fab

Structural highlights

1ors is a 3 chain structure with sequence from Aeropyrum pernix and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

IGKC_MOUSE

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

Voltage-dependent K+ channels are members of the family of voltage-dependent cation (K+, Na+ and Ca2+) channels that open and allow ion conduction in response to changes in cell membrane voltage. This form of gating underlies the generation of nerve and muscle action potentials, among other processes. Here we present the structure of KvAP, a voltage-dependent K+ channel from Aeropyrum pernix. We have determined a crystal structure of the full-length channel at a resolution of 3.2 A, and of the isolated voltage-sensor domain at 1.9 A, both in complex with monoclonal Fab fragments. The channel contains a central ion-conduction pore surrounded by voltage sensors, which form what we call 'voltage-sensor paddles'-hydrophobic, cationic, helix-turn-helix structures on the channel's outer perimeter. Flexible hinges suggest that the voltage-sensor paddles move in response to membrane voltage changes, carrying their positive charge across the membrane.

X-ray structure of a voltage-dependent K+ channel.,Jiang Y, Lee A, Chen J, Ruta V, Cadene M, Chait BT, MacKinnon R Nature. 2003 May 1;423(6935):33-41. PMID:12721618^[1]

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

References

↑ Jiang Y, Lee A, Chen J, Ruta V, Cadene M, Chait BT, MacKinnon R. X-ray structure of a voltage-dependent K+ channel. Nature. 2003 May 1;423(6935):33-41. PMID:12721618 doi:http://dx.doi.org/10.1038/nature01580

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/1ors"

@@ Line 3: / Line 3: @@
 <StructureSection load='1ors' size='340' side='right'caption='[[1ors]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ors]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Aerpx Aerpx] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ORS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ORS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ors]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ORS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ORS FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1orq|1orq]]</div></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</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=1ors FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ors OCA], [https://pdbe.org/1ors PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ors RCSB], [https://www.ebi.ac.uk/pdbsum/1ors PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ors ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/KVAP_AERPE KVAP_AERPE]] Mediates a strong voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.
+[https://www.uniprot.org/uniprot/IGKC_MOUSE IGKC_MOUSE]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Aerpx]]
+[[Category: Aeropyrum pernix]]
 [[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Cadene, M]]
+[[Category: Cadene M]]
-[[Category: Chait, B T]]
+[[Category: Chait BT]]
-[[Category: Chen, J]]
+[[Category: Chen J]]
-[[Category: Jiang, Y]]
+[[Category: Jiang Y]]
-[[Category: Lee, A]]
+[[Category: Lee A]]
-[[Category: MacKinnon, R]]
+[[Category: MacKinnon R]]
-[[Category: Ruta, V]]
+[[Category: Ruta V]]
-[[Category: Fab complex]]
-[[Category: Kvap]]
-[[Category: Membrane protein]]
-[[Category: Potassium channel]]
-[[Category: Voltage sensor]]
-[[Category: Voltage-dependent]]

1ors

From Proteopedia

Current revision

X-ray structure of the KvAP potassium channel voltage sensor in complex with an Fab

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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