2a0l
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2a0l.jpg|left|200px]] | [[Image:2a0l.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2a0l", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_2a0l| PDB=2a0l | SCENE= }} | |
| - | | | + | |
| - | + | ||
| - | }} | + | |
'''Crystal structure of KvAP-33H1 Fv complex''' | '''Crystal structure of KvAP-33H1 Fv complex''' | ||
| Line 30: | Line 27: | ||
[[Category: Lee, S Y.]] | [[Category: Lee, S Y.]] | ||
[[Category: Mackinnon, R.]] | [[Category: Mackinnon, R.]] | ||
| - | [[Category: | + | [[Category: Ion channel]] |
| - | [[Category: | + | [[Category: K+ channel-fv complex]] |
| - | [[Category: | + | [[Category: Membrane protein]] |
| - | [[Category: | + | [[Category: Voltage sensor]] |
| - | [[Category: | + | [[Category: Voltage-dependent k+ channel]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:27:32 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 15:27, 3 May 2008
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
