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[[Image:2a0l.jpg|left|200px]]
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{{STRUCTURE_2a0l|  PDB=2a0l  |  SCENE=  }}
'''Crystal structure of KvAP-33H1 Fv complex'''


==Crystal structure of KvAP-33H1 Fv complex==
<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 [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='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='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='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>
</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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a0/2a0l_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2a0l ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==Overview==
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<ref>PMID:16223877</ref>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2A0L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix] 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].
</div>
<div class="pdbe-citations 2a0l" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/16223877 16223877]
*[[Potassium channel 3D structures|Potassium channel 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aeropyrum pernix]]
[[Category: Aeropyrum pernix]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Chen J]]
[[Category: Chen, J.]]
[[Category: Lee A]]
[[Category: Lee, A.]]
[[Category: Lee SY]]
[[Category: Lee, S Y.]]
[[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]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 18:27:32 2008''

Latest revision as of 07:47, 30 October 2024

Crystal structure of KvAP-33H1 Fv complex

2a0l, resolution 3.90Å

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