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2a0l

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[[Image:2a0l.jpg|left|200px]]
[[Image:2a0l.jpg|left|200px]]
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{{Structure
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|PDB= 2a0l |SIZE=350|CAPTION= <scene name='initialview01'>2a0l</scene>, resolution 3.90&Aring;
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The line below this paragraph, containing "STRUCTURE_2a0l", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>
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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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{{STRUCTURE_2a0l| PDB=2a0l | SCENE= }}
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|RELATEDENTRY=[[1orq|1ORQ]]
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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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'''Crystal structure of KvAP-33H1 Fv complex'''
'''Crystal structure of KvAP-33H1 Fv complex'''
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[[Category: Lee, S Y.]]
[[Category: Lee, S Y.]]
[[Category: Mackinnon, R.]]
[[Category: Mackinnon, R.]]
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[[Category: ion channel]]
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[[Category: Ion channel]]
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[[Category: k+ channel-fv complex]]
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[[Category: K+ channel-fv complex]]
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[[Category: membrane protein]]
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[[Category: Membrane protein]]
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[[Category: voltage sensor]]
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[[Category: Voltage sensor]]
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[[Category: voltage-dependent k+ channel]]
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[[Category: Voltage-dependent k+ channel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:27:32 2008''
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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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Revision as of 15:27, 3 May 2008

Template:STRUCTURE 2a0l

Crystal structure of KvAP-33H1 Fv complex


Overview

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

2A0L is a Single protein structure of sequence from Aeropyrum pernix and Mus musculus. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sat May 3 18:27:32 2008

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