2a0l
From Proteopedia
(New page: 200px<br /><applet load="2a0l" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a0l, resolution 3.90Å" /> '''Crystal structure of...) |
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| - | [[Image:2a0l.jpg|left|200px]]<br /><applet load="2a0l" size=" | + | [[Image:2a0l.jpg|left|200px]]<br /><applet load="2a0l" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2a0l, resolution 3.90Å" /> | caption="2a0l, resolution 3.90Å" /> | ||
'''Crystal structure of KvAP-33H1 Fv complex'''<br /> | '''Crystal structure of KvAP-33H1 Fv complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Voltage-dependent ion channels gate open in response to changes in cell | + | 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== | ==About this Structure== | ||
| - | 2A0L is a [http://en.wikipedia.org/wiki/Single_protein 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] with K as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2A0L is a [http://en.wikipedia.org/wiki/Single_protein 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] with <scene name='pdbligand=K:'>K</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A0L OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Chen, J.]] | [[Category: Chen, J.]] | ||
[[Category: Lee, A.]] | [[Category: Lee, A.]] | ||
| - | [[Category: Lee, S | + | [[Category: Lee, S Y.]] |
[[Category: Mackinnon, R.]] | [[Category: Mackinnon, R.]] | ||
[[Category: K]] | [[Category: K]] | ||
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[[Category: voltage-dependent k+ channel]] | [[Category: voltage-dependent k+ channel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:22:32 2008'' |
Revision as of 14:22, 21 February 2008
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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 with as ligand. 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
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