2k72: Difference between revisions
New page: '''Unreleased structure''' The entry 2k72 is ON HOLD Authors: Rangaraju, S.K., Khoo, K.K., Feng, Z., Crossley, G., Norton, R.S., Chandy, G.K. Description: MMP23, a metalloprotease with... |
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==Solution NMR structure of toxin-like potassium channel blocking domain in MMP23== | |||
<StructureSection load='2k72' size='340' side='right'caption='[[2k72]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2k72]] 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=2K72 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K72 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=2k72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k72 OCA], [https://pdbe.org/2k72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k72 RCSB], [https://www.ebi.ac.uk/pdbsum/2k72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k72 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MMP23_RAT MMP23_RAT] Protease. May regulate the surface expression of some potassium channels by retaining them in the endoplasmic reticulum.<ref>PMID:19965868</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Peptide toxins found in a wide array of venoms block K(+) channels, causing profound physiological and pathological effects. Here we describe the first functional K(+) channel-blocking toxin domain in a mammalian protein. MMP23 (matrix metalloprotease 23) contains a domain (MMP23(TxD)) that is evolutionarily related to peptide toxins from sea anemones. MMP23(TxD) shows close structural similarity to the sea anemone toxins BgK and ShK. Moreover, this domain blocks K(+) channels in the nanomolar to low micromolar range (Kv1.6 > Kv1.3 > Kv1.1 = Kv3.2 > Kv1.4, in decreasing order of potency) while sparing other K(+) channels (Kv1.2, Kv1.5, Kv1.7, and KCa3.1). Full-length MMP23 suppresses K(+) channels by co-localizing with and trapping MMP23(TxD)-sensitive channels in the ER. Our results provide clues to the structure and function of the vast family of proteins that contain domains related to sea anemone toxins. Evolutionary pressure to maintain a channel-modulatory function may contribute to the conservation of this domain throughout the plant and animal kingdoms. | |||
Potassium channel modulation by a toxin domain in matrix metalloprotease 23.,Rangaraju S, Khoo KK, Feng ZP, Crossley G, Nugent D, Khaytin I, Chi V, Pham C, Calabresi P, Pennington MW, Norton RS, Chandy KG J Biol Chem. 2010 Mar 19;285(12):9124-36. Epub 2009 Dec 4. PMID:19965868<ref>PMID:19965868</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2k72" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Rattus norvegicus]] | |||
[[Category: Feng Z]] | |||
[[Category: Khoo KK]] | |||
[[Category: Norton RS]] | |||
Latest revision as of 12:14, 6 November 2024
Solution NMR structure of toxin-like potassium channel blocking domain in MMP23Solution NMR structure of toxin-like potassium channel blocking domain in MMP23
Structural highlights
FunctionMMP23_RAT Protease. May regulate the surface expression of some potassium channels by retaining them in the endoplasmic reticulum.[1] Publication Abstract from PubMedPeptide toxins found in a wide array of venoms block K(+) channels, causing profound physiological and pathological effects. Here we describe the first functional K(+) channel-blocking toxin domain in a mammalian protein. MMP23 (matrix metalloprotease 23) contains a domain (MMP23(TxD)) that is evolutionarily related to peptide toxins from sea anemones. MMP23(TxD) shows close structural similarity to the sea anemone toxins BgK and ShK. Moreover, this domain blocks K(+) channels in the nanomolar to low micromolar range (Kv1.6 > Kv1.3 > Kv1.1 = Kv3.2 > Kv1.4, in decreasing order of potency) while sparing other K(+) channels (Kv1.2, Kv1.5, Kv1.7, and KCa3.1). Full-length MMP23 suppresses K(+) channels by co-localizing with and trapping MMP23(TxD)-sensitive channels in the ER. Our results provide clues to the structure and function of the vast family of proteins that contain domains related to sea anemone toxins. Evolutionary pressure to maintain a channel-modulatory function may contribute to the conservation of this domain throughout the plant and animal kingdoms. Potassium channel modulation by a toxin domain in matrix metalloprotease 23.,Rangaraju S, Khoo KK, Feng ZP, Crossley G, Nugent D, Khaytin I, Chi V, Pham C, Calabresi P, Pennington MW, Norton RS, Chandy KG J Biol Chem. 2010 Mar 19;285(12):9124-36. Epub 2009 Dec 4. PMID:19965868[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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