1jo6

From Proteopedia

(Difference between revisions)

Current revision

Solution structure of the cytoplasmic N-terminus of the BK beta-subunit KCNMB2

Structural highlights

1jo6 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KCMB2_HUMAN Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Acts as a negative regulator that confers rapid and complete inactivation of KCNMA1 channel complex. May participate in KCNMA1 inactivation in chromaffin cells of the adrenal gland or in hippocampal CA1 neurons.^[1] ^[2]

Publication Abstract from PubMed

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Wallner M, Meera P, Toro L. Molecular basis of fast inactivation in voltage and Ca2+-activated K+ channels: a transmembrane beta-subunit homolog. Proc Natl Acad Sci U S A. 1999 Mar 30;96(7):4137-42. PMID:10097176
↑ Xia XM, Ding JP, Lingle CJ. Molecular basis for the inactivation of Ca2+- and voltage-dependent BK channels in adrenal chromaffin cells and rat insulinoma tumor cells. J Neurosci. 1999 Jul 1;19(13):5255-64. PMID:10377337
↑ Bentrop D, Beyermann M, Wissmann R, Fakler B. NMR structure of the "ball-and-chain" domain of KCNMB2, the beta 2-subunit of large conductance Ca2+- and voltage-activated potassium channels. J Biol Chem. 2001 Nov 9;276(45):42116-21. Epub 2001 Aug 21. PMID:11517232 doi:10.1074/jbc.M107118200

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1jo6"

@@ Line 1: / Line 1: @@
 ==Solution structure of the cytoplasmic N-terminus of the BK beta-subunit KCNMB2==
-<StructureSection load='1jo6' size='340' side='right'caption='[[1jo6]], [[NMR_Ensembles_of_Models | 24 NMR models]]' scene=''>
+<StructureSection load='1jo6' size='340' side='right'caption='[[1jo6]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1jo6]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JO6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JO6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1jo6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JO6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JO6 FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jo6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jo6 OCA], [https://pdbe.org/1jo6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jo6 RCSB], [https://www.ebi.ac.uk/pdbsum/1jo6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jo6 ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jo6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jo6 OCA], [https://pdbe.org/1jo6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jo6 RCSB], [https://www.ebi.ac.uk/pdbsum/1jo6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jo6 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/KCMB2_HUMAN KCMB2_HUMAN]] Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Acts as a negative regulator that confers rapid and complete inactivation of KCNMA1 channel complex. May participate in KCNMA1 inactivation in chromaffin cells of the adrenal gland or in hippocampal CA1 neurons.<ref>PMID:10097176</ref> <ref>PMID:10377337</ref>
+[https://www.uniprot.org/uniprot/KCMB2_HUMAN KCMB2_HUMAN] Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Acts as a negative regulator that confers rapid and complete inactivation of KCNMA1 channel complex. May participate in KCNMA1 inactivation in chromaffin cells of the adrenal gland or in hippocampal CA1 neurons.<ref>PMID:10097176</ref> <ref>PMID:10377337</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 25: @@
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Bentrop, D]]
+[[Category: Bentrop D]]
-[[Category: Beyermann, M]]
+[[Category: Beyermann M]]
-[[Category: Fakler, B]]
+[[Category: Fakler B]]
-[[Category: Wissmann, R]]
+[[Category: Wissmann R]]
-[[Category: Cytoplasmic part of]]
-[[Category: Helix]]
-[[Category: Ion channel]]
-[[Category: Membrane protein]]
-[[Category: Metal transport]]

1jo6

From Proteopedia

Current revision

Solution structure of the cytoplasmic N-terminus of the BK beta-subunit KCNMB2

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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