1jo6
From Proteopedia
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[[Image:1jo6.gif|left|200px]] | [[Image:1jo6.gif|left|200px]] | ||
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| - | + | {{STRUCTURE_1jo6| PDB=1jo6 | SCENE= }} | |
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'''Solution structure of the cytoplasmic N-terminus of the BK beta-subunit KCNMB2''' | '''Solution structure of the cytoplasmic N-terminus of the BK beta-subunit KCNMB2''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1JO6 is a [[Single protein]] structure | + | 1JO6 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JO6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Fakler, B.]] | [[Category: Fakler, B.]] | ||
[[Category: Wissmann, R.]] | [[Category: Wissmann, R.]] | ||
| - | [[Category: | + | [[Category: Cytoplasmic part of]] |
| - | [[Category: | + | [[Category: Helix]] |
| - | [[Category: | + | [[Category: Ion channel]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:29:34 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 18:29, 2 May 2008
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. 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 Fri May 2 21:29:34 2008
