2A0L

Crystal structure of KvAP-33H1 Fv complex

Summary for 2A0L

• Entry DOI: 10.2210/pdb2a0l/pdb
• Related: 1ORQ
• Descriptor: Voltage-gated potassium channel, 33H1 Fv fragment, POTASSIUM ION, ... (4 entities in total)
• Functional Keywords: voltage sensor, voltage-dependent k+ channel, k+ channel-fv complex, membrane protein, ion channel
• Biological source: Aeropyrum pernix; More
• Cellular location: Cell membrane; Multi-pass membrane protein: Q9YDF8
• Total number of polymer chains: 6
• Total formula weight: 101334.28

Authors

Lee, S.Y.,Lee, A.,Chen, J.,Mackinnon, R. (deposition date: 2005-06-16, release date: 2005-11-01, Last modification date: 2024-10-30)

Primary citation

Lee, S.Y.,Lee, A.,Chen, J.,Mackinnon, R.
Structure of the KvAP voltage-dependent K+ channel and its dependence on the lipid membrane.
Proc.Natl.Acad.Sci.Usa, 102:15441-15446, 2005

PubMed Abstract: 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.

PubMed: 16223877
DOI: 10.1073/pnas.0507651102

Experimental method

X-RAY DIFFRACTION (3.9 Å)