1kkd

From Proteopedia

(Difference between revisions)

Current revision

Solution structure of the calmodulin binding domain (CaMBD) of small conductance Ca2+-activated potassium channels (SK2)

Structural highlights

1kkd is a 1 chain structure with sequence from Rattus norvegicus. 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

KCNN2_RAT Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Small conductance Ca(2+)-activated potassium (SK) channels underlie the afterhyperpolarization that follows the action potential in many types of central neurons. SK channels are voltage-independent and gated solely by intracellular Ca(2+) in the submicromolar range. This high affinity for Ca(2+) results from Ca(2+)-independent association of the SK alpha-subunit with calmodulin (CaM), a property unique among the large family of potassium channels. Here we report the solution structure of the calmodulin binding domain (CaMBD, residues 396-487 in rat SK2) of SK channels using NMR spectroscopy. The CaMBD exhibits a helical region between residues 423-437, whereas the rest of the molecule lacks stable overall folding. Disruption of the helical domain abolishes constitutive association of CaMBD with Ca(2+)-free CaM, and results in SK channels that are no longer gated by Ca(2+). The results show that the Ca(2+)-independent CaM-CaMBD interaction, which is crucial for channel function, is at least in part determined by a region different in sequence and structure from other CaM-interacting proteins.

A helical region in the C terminus of small-conductance Ca2+-activated K+ channels controls assembly with apo-calmodulin.,Wissmann R, Bildl W, Neumann H, Rivard AF, Klocker N, Weitz D, Schulte U, Adelman JP, Bentrop D, Fakler B J Biol Chem. 2002 Feb 8;277(6):4558-64. Epub 2001 Nov 26. PMID:11723128^[1]

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

References

↑ Wissmann R, Bildl W, Neumann H, Rivard AF, Klocker N, Weitz D, Schulte U, Adelman JP, Bentrop D, Fakler B. A helical region in the C terminus of small-conductance Ca2+-activated K+ channels controls assembly with apo-calmodulin. J Biol Chem. 2002 Feb 8;277(6):4558-64. Epub 2001 Nov 26. PMID:11723128 doi:http://dx.doi.org/10.1074/jbc.M109240200

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Solution structure of the calmodulin binding domain (CaMBD) of small conductance Ca2+-activated potassium channels (SK2)==
-<StructureSection load='1kkd' size='340' side='right'caption='[[1kkd]], [[NMR_Ensembles_of_Models | 23 NMR models]]' scene=''>
+<StructureSection load='1kkd' size='340' side='right'caption='[[1kkd]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1kkd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KKD FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1kkd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KKD FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1g4y|1g4y]]</div></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SK2 (KCNN2) ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=1kkd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kkd OCA], [https://pdbe.org/1kkd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kkd RCSB], [https://www.ebi.ac.uk/pdbsum/1kkd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kkd ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/KCNN2_RAT KCNN2_RAT]] Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin.
+[https://www.uniprot.org/uniprot/KCNN2_RAT KCNN2_RAT] Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 36: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Buffalo rat]]
 [[Category: Large Structures]]
-[[Category: Adelman, J P]]
+[[Category: Rattus norvegicus]]
-[[Category: Bentrop, D]]
+[[Category: Adelman JP]]
-[[Category: Bildl, W]]
+[[Category: Bentrop D]]
-[[Category: Fakler, B]]
+[[Category: Bildl W]]
-[[Category: Kloecker, N]]
+[[Category: Fakler B]]
-[[Category: Neumann, H]]
+[[Category: Kloecker N]]
-[[Category: Rivard, A F]]
+[[Category: Neumann H]]
-[[Category: Schulte, U]]
+[[Category: Rivard AF]]
-[[Category: Weitz, D]]
+[[Category: Schulte U]]
-[[Category: Wissmann, R]]
+[[Category: Weitz D]]
-[[Category: Channel gating]]
+[[Category: Wissmann R]]
-[[Category: Signaling protein]]
-[[Category: Small-conductance calcium-activated potassium channel]]

1kkd

From Proteopedia

Current revision

Solution structure of the calmodulin binding domain (CaMBD) of small conductance Ca2+-activated potassium channels (SK2)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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