1jo6
From Proteopedia
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| - | [[Image:1jo6.gif|left|200px]] | + | [[Image:1jo6.gif|left|200px]] |
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| - | '''Solution structure of the cytoplasmic N-terminus of the BK beta-subunit KCNMB2''' | + | {{Structure |
| + | |PDB= 1jo6 |SIZE=350|CAPTION= <scene name='initialview01'>1jo6</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Solution structure of the cytoplasmic N-terminus of the BK beta-subunit KCNMB2''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1JO6 is a [ | + | 1JO6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JO6 OCA]. |
==Reference== | ==Reference== | ||
| - | NMR structure of the "ball-and-chain" domain of KCNMB2, the beta 2-subunit of large conductance Ca2+- and voltage-activated potassium channels., Bentrop D, Beyermann M, Wissmann R, Fakler B, J Biol Chem. 2001 Nov 9;276(45):42116-21. Epub 2001 Aug 21. PMID:[http:// | + | NMR structure of the "ball-and-chain" domain of KCNMB2, the beta 2-subunit of large conductance Ca2+- and voltage-activated potassium channels., Bentrop D, Beyermann M, Wissmann R, Fakler B, J Biol Chem. 2001 Nov 9;276(45):42116-21. Epub 2001 Aug 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11517232 11517232] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bentrop, D.]] | [[Category: Bentrop, D.]] | ||
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[[Category: ion channel]] | [[Category: ion 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 12:06:04 2008'' |
Revision as of 10:06, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of the cytoplasmic N-terminus of the BK beta-subunit KCNMB2
Overview
The auxiliary beta-subunit KCNMB2 (beta(2)) endows the non-inactivating large conductance Ca(2+)- and voltage-dependent potassium (BK) channel with fast inactivation. This process is mediated by the N terminus of KCNMB2 and closely resembles the "ball-and-chain"-type inactivation observed in voltage-gated potassium channels. Here we investigated the solution structure and function of the KCNMB2 N terminus (amino acids 1-45, BKbeta(2)N) using NMR spectroscopy and patch clamp recordings. BKbeta(2)N completely inactivated BK channels when applied to the cytoplasmic side; its interaction with the BK alpha-subunit is characterized by a particularly slow dissociation rate and an affinity in the upper nanomolar range. The BKbeta(2)N structure comprises two domains connected by a flexible linker: the pore-blocking "ball domain" (formed by residues 1-17) and the "chain domain" (between residues 20-45) linking it to the membrane segment of KCNMB2. The ball domain is made up of a flexible N terminus anchored at a well ordered loop-helix motif. The chain domain consists of a 4-turn helix with an unfolded linker at its C terminus. These structural properties explain the functional characteristics of BKbeta(2)N-mediated inactivation.
About this Structure
1JO6 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
NMR structure of the "ball-and-chain" domain of KCNMB2, the beta 2-subunit of large conductance Ca2+- and voltage-activated potassium channels., Bentrop D, Beyermann M, Wissmann R, Fakler B, J Biol Chem. 2001 Nov 9;276(45):42116-21. Epub 2001 Aug 21. PMID:11517232
Page seeded by OCA on Thu Mar 20 12:06:04 2008
