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| [[Image:1jo6.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1jo6| PDB=1jo6 | SCENE= }} | | {{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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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_11517232}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11517232 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11517232}} |
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| ==About this Structure== | | ==About this Structure== |
| 1JO6 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JO6 OCA]. | | 1JO6 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JO6 OCA]. |
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| ==Reference== | | ==Reference== |
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| [[Category: Helix]] | | [[Category: Helix]] |
| [[Category: Ion channel]] | | [[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 Tue Jul 1 20:32:39 2008'' |
