2a0l
From Proteopedia
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- | [[Image:2a0l.jpg|left|200px]] | + | [[Image:2a0l.jpg|left|200px]] |
- | + | ||
- | '''Crystal structure of KvAP-33H1 Fv complex''' | + | {{Structure |
+ | |PDB= 2a0l |SIZE=350|CAPTION= <scene name='initialview01'>2a0l</scene>, resolution 3.90Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=K:POTASSIUM ION'>K</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= KVAP_AERPE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=56636 Aeropyrum pernix]) | ||
+ | }} | ||
+ | |||
+ | '''Crystal structure of KvAP-33H1 Fv complex''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2A0L is a [ | + | 2A0L is a [[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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A0L OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16223877 16223877] |
[[Category: Aeropyrum pernix]] | [[Category: Aeropyrum pernix]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
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[[Category: voltage-dependent k+ channel]] | [[Category: voltage-dependent k+ channel]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:44:06 2008'' |
Revision as of 13:44, 20 March 2008
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, resolution 3.90Å | |||||||
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Ligands: | |||||||
Gene: | KVAP_AERPE (Aeropyrum pernix) | ||||||
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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