2a0l

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[[Image:2a0l.jpg|left|200px]]
 
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{{Structure
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==Crystal structure of KvAP-33H1 Fv complex==
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|PDB= 2a0l |SIZE=350|CAPTION= <scene name='initialview01'>2a0l</scene>, resolution 3.90&Aring;
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<StructureSection load='2a0l' size='340' side='right'caption='[[2a0l]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>
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<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>
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|ACTIVITY=
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</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>
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|GENE= KVAP_AERPE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=56636 Aeropyrum pernix])
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<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>
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|DOMAIN=
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<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>
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|RELATEDENTRY=[[1orq|1ORQ]]
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</table>
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|RESOURCES=<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://www.ebi.ac.uk/pdbsum/2a0l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2a0l RCSB]</span>
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== Function ==
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}}
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a0/2a0l_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''Crystal structure of KvAP-33H1 Fv complex'''
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2a0l" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Potassium channel 3D structures|Potassium channel 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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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].
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__TOC__
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</StructureSection>
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==Reference==
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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]
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[[Category: Aeropyrum pernix]]
[[Category: Aeropyrum pernix]]
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Chen J]]
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[[Category: Chen, J.]]
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[[Category: Lee A]]
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[[Category: Lee, A.]]
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[[Category: Lee SY]]
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[[Category: Lee, S Y.]]
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[[Category: Mackinnon R]]
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[[Category: Mackinnon, R.]]
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[[Category: ion channel]]
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[[Category: k+ channel-fv complex]]
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[[Category: membrane protein]]
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[[Category: voltage sensor]]
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[[Category: voltage-dependent k+ channel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:46:18 2008''
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Current revision

Crystal structure of KvAP-33H1 Fv complex

PDB ID 2a0l

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