2k72: Difference between revisions
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==Solution NMR structure of toxin-like potassium channel blocking domain in MMP23== | ==Solution NMR structure of toxin-like potassium channel blocking domain in MMP23== | ||
<StructureSection load='2k72' size='340' side='right' caption='[[2k72]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2k72' size='340' side='right'caption='[[2k72]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2k72]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K72 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2k72]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K72 FirstGlance]. <br> | ||
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==See Also== | ==See Also== | ||
*[[Matrix metalloproteinase|Matrix metalloproteinase]] | *[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Feng, Z]] | [[Category: Feng, Z]] | ||
[[Category: Khoo, K K]] | [[Category: Khoo, K K]] | ||
Revision as of 09:56, 19 February 2020
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
Function[MMP23_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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