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2a0l

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Crystal structure of KvAP-33H1 Fv complex

Structural highlights

2a0l is a 6 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 3.9Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

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 ion channels gate open in response to changes in cell membrane voltage. This form of gating permits the propagation of action potentials. We present two structures of the voltage-dependent K(+) channel KvAP, in complex with monoclonal Fv fragments (3.9 A) and without antibody fragments (8 A). We also studied KvAP with disulfide cross-bridges in lipid membranes. Analyzing these data in the context of the crystal structure of Kv1.2 and EPR data on KvAP we reach the following conclusions: (i) KvAP is similar in structure to Kv1.2 with a very modest difference in the orientation of its voltage sensor; (ii) mAb fragments are not the source of non-native conformations of KvAP in crystal structures; (iii) because KvAP contains separate loosely adherent domains, a lipid membrane is required to maintain their correct relative orientations, and (iv) the model of KvAP is consistent with the proposal of voltage sensing through the movement of an arginine-containing helix-turn-helix element at the protein-lipid interface.

Structure of the KvAP voltage-dependent K+ channel and its dependence on the lipid membrane.,Lee SY, Lee A, Chen J, MacKinnon R Proc Natl Acad Sci U S A. 2005 Oct 25;102(43):15441-6. Epub 2005 Oct 13. PMID:16223877^[1]

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

References

↑ Lee SY, Lee A, Chen J, MacKinnon R. Structure of the KvAP voltage-dependent K+ channel and its dependence on the lipid membrane. Proc Natl Acad Sci U S A. 2005 Oct 25;102(43):15441-6. Epub 2005 Oct 13. PMID:16223877

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/2a0l"

@@ Line 1: / Line 1: @@
 ==Crystal structure of KvAP-33H1 Fv complex==
-<StructureSection load='2a0l' size='340' side='right' caption='[[2a0l]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
+<StructureSection load='2a0l' size='340' side='right'caption='[[2a0l]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2a0l]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Aerpx Aerpx] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A0L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2A0L FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2a0l]] is a 6 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=2A0L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A0L FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></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]] 3.9&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1orq|1orq]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KVAP_AERPE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=56636 AERPX])</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=2a0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a0l OCA], [https://pdbe.org/2a0l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a0l RCSB], [https://www.ebi.ac.uk/pdbsum/2a0l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a0l ProSAT]</span></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=2a0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a0l OCA], [http://pdbe.org/2a0l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2a0l RCSB], [http://www.ebi.ac.uk/pdbsum/2a0l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2a0l ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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/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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 31: @@
 ==See Also==
-*[[Potassium Channel|Potassium Channel]]
+*[[Potassium channel 3D structures|Potassium channel 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Aerpx]]
+[[Category: Aeropyrum pernix]]
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Chen, J]]
+[[Category: Chen J]]
-[[Category: Lee, A]]
+[[Category: Lee A]]
-[[Category: Lee, S Y]]
+[[Category: Lee SY]]
-[[Category: Mackinnon, R]]
+[[Category: Mackinnon R]]
-[[Category: Ion channel]]
-[[Category: K+ channel-fv complex]]
-[[Category: Membrane protein]]
-[[Category: Voltage sensor]]
-[[Category: Voltage-dependent k+ channel]]

2a0l

From Proteopedia

Current revision

Crystal structure of KvAP-33H1 Fv complex

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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