2a0l
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(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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Revision as of 05:44, 21 November 2007
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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 K 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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