9zrk: Difference between revisions

Latest revision as of 05:42, 27 May 2026

Cryo-EM structure of KCa3.1_I/calmodulin channel in complex with SKA111.

Structural highlights

9zrk is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 2.99Å
Ligands:	A1C3U, CA, K
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

KCNN4_HUMAN The disease is caused by mutations affecting the gene represented in this entry.

Function

KCNN4_HUMAN Forms a voltage-independent potassium channel that is activated by intracellular calcium (PubMed:26148990). Activation is followed by membrane hyperpolarization which promotes calcium influx. Required for maximal calcium influx and proliferation during the reactivation of naive T-cells. The channel is blocked by clotrimazole and charybdotoxin but is insensitive to apamin (PubMed:17157250, PubMed:18796614).^[1] ^[2] ^[3]

References

↑ Srivastava S, Li Z, Ko K, Choudhury P, Albaqumi M, Johnson AK, Yan Y, Backer JM, Unutmaz D, Coetzee WA, Skolnik EY. Histidine phosphorylation of the potassium channel KCa3.1 by nucleoside diphosphate kinase B is required for activation of KCa3.1 and CD4 T cells. Mol Cell. 2006 Dec 8;24(5):665-675. doi: 10.1016/j.molcel.2006.11.012. PMID:17157250 doi:https://dx.doi.org/10.1016/j.molcel.2006.11.012
↑ Srivastava S, Zhdanova O, Di L, Li Z, Albaqumi M, Wulff H, Skolnik EY. Protein histidine phosphatase 1 negatively regulates CD4 T cells by inhibiting the K+ channel KCa3.1. Proc Natl Acad Sci U S A. 2008 Sep 23;105(38):14442-6. doi:, 10.1073/pnas.0803678105. Epub 2008 Sep 16. PMID:18796614 doi:https://dx.doi.org/10.1073/pnas.0803678105
↑ Rapetti-Mauss R, Lacoste C, Picard V, Guitton C, Lombard E, Loosveld M, Nivaggioni V, Dasilva N, Salgado D, Desvignes JP, Beroud C, Viout P, Bernard M, Soriani O, Vinti H, Lacroze V, Feneant-Thibault M, Thuret I, Guizouarn H, Badens C. A mutation in the Gardos channel is associated with hereditary xerocytosis. Blood. 2015 Sep 10;126(11):1273-80. doi: 10.1182/blood-2015-04-642496. Epub 2015 , Jul 6. PMID:26148990 doi:https://dx.doi.org/10.1182/blood-2015-04-642496

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OCA

[1] Srivastava S, Li Z, Ko K, Choudhury P, Albaqumi M, Johnson AK, Yan Y, Backer JM, Unutmaz D, Coetzee WA, Skolnik EY. Histidine phosphorylation of the potassium channel KCa3.1 by nucleoside diphosphate kinase B is required for activation of KCa3.1 and CD4 T cells. Mol Cell. 2006 Dec 8;24(5):665-675. doi: 10.1016/j.molcel.2006.11.012. PMID:17157250 doi:https://dx.doi.org/10.1016/j.molcel.2006.11.012

[2] Srivastava S, Zhdanova O, Di L, Li Z, Albaqumi M, Wulff H, Skolnik EY. Protein histidine phosphatase 1 negatively regulates CD4 T cells by inhibiting the K+ channel KCa3.1. Proc Natl Acad Sci U S A. 2008 Sep 23;105(38):14442-6. doi:, 10.1073/pnas.0803678105. Epub 2008 Sep 16. PMID:18796614 doi:https://dx.doi.org/10.1073/pnas.0803678105

[3] Rapetti-Mauss R, Lacoste C, Picard V, Guitton C, Lombard E, Loosveld M, Nivaggioni V, Dasilva N, Salgado D, Desvignes JP, Beroud C, Viout P, Bernard M, Soriani O, Vinti H, Lacroze V, Feneant-Thibault M, Thuret I, Guizouarn H, Badens C. A mutation in the Gardos channel is associated with hereditary xerocytosis. Blood. 2015 Sep 10;126(11):1273-80. doi: 10.1182/blood-2015-04-642496. Epub 2015 , Jul 6. PMID:26148990 doi:https://dx.doi.org/10.1182/blood-2015-04-642496

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[3]

@@ Line 5: / Line 5: @@
 <table><tr><td colspan='2'>[[9zrk]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9ZRK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9ZRK FirstGlance]. <br>
 </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.99&#8491;</td></tr>
-<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1C3U:5-methylbenzo[e][1,3]benzothiazol-2-amine'>A1C3U</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1C3U:5-methylnaphtho[1,2-d][1,3]thiazol-2-amine'>A1C3U</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></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=9zrk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9zrk OCA], [https://pdbe.org/9zrk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9zrk RCSB], [https://www.ebi.ac.uk/pdbsum/9zrk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9zrk ProSAT]</span></td></tr>
 </table>

9zrk: Difference between revisions

Latest revision as of 05:42, 27 May 2026

Cryo-EM structure of KCa3.1_I/calmodulin channel in complex with SKA111.

Structural highlights

Disease

Function

References

Contents

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