2a0l
From Proteopedia
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|PDB= 2a0l |SIZE=350|CAPTION= <scene name='initialview01'>2a0l</scene>, resolution 3.90Å | |PDB= 2a0l |SIZE=350|CAPTION= <scene name='initialview01'>2a0l</scene>, resolution 3.90Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=K:POTASSIUM ION'>K</scene> | + | |LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= KVAP_AERPE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=56636 Aeropyrum pernix]) | |GENE= KVAP_AERPE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=56636 Aeropyrum pernix]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1orq|1ORQ]] | ||
| + | |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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[[Category: Lee, S Y.]] | [[Category: Lee, S Y.]] | ||
[[Category: Mackinnon, R.]] | [[Category: Mackinnon, R.]] | ||
| - | [[Category: K]] | ||
[[Category: ion channel]] | [[Category: ion channel]] | ||
[[Category: k+ channel-fv complex]] | [[Category: k+ channel-fv complex]] | ||
| Line 34: | Line 36: | ||
[[Category: voltage-dependent k+ channel]] | [[Category: voltage-dependent k+ channel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:46:18 2008'' |
Revision as of 22:46, 30 March 2008
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| , resolution 3.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | KVAP_AERPE (Aeropyrum pernix) | ||||||
| Related: | 1ORQ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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