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KCNA1 binds kcsA. 28 / 28
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"In accordance with these data, our recombinant ChTx competes partially with R-AgTx2 for the binding to KcsA-Kv1.3 and does not disturb R-AgTx2 bound to KcsA-Kv1.1 even at the 400 nM concentration ( Fi[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Recombinant ScTx does not bind to KcsA-Kv1.1 or KcsA-Kv1.3 ( Fig. 4 E), since it is a specific blocker of K Ca 2.3 channel ( http://kaliumdb.org )."
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"In contrast to N-terminally tagged AgTx2, AgTx2-L3-GFP was found to interact with KcsA-Kv1.1 and KcsA-Kv1.6, as well as with KcsA-Kv1.3 ( xref )."
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"At the same conditions, formation of His6-GFP-L2-AgTx2 complexes with KcsA-Kv1.1 and KcsA-Kv1.6 was not observed even after addition of 250 nM His6-GFP-L2-AgTx2."
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"Thus, under conditions optimized for KcsA-Kv1.3 production, the total protein levels of KcsA-Kv1.1 and KcsA-Kv1.6 chimeras were found to be threefold [34] and twofold [44] lower in comparison to KcsA-[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Therefore, we designed and successfully produced advanced KcsA-Kv1.3, KcsA-Kv1.1, and KcsA-Kv1.2 chimeric proteins in which both the turret and part of the filter regions of the human Kv1."
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"Therefore, the similarly low intensity of A-AgTx2 fluorescence recorded from control spheroplasts and spheroplasts bearing the KcsA–Kv1.1 or KcsA–Kv1.6 channels ( xref B) can be explained by the inability of A-AgTx2 to interact with the Kv1.1 and Kv1.6 binding sites."
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"Spheroplasts of E. coli cells expressing KcsA-Kv1.1 or KcsA-Kv1.3 hybrid channels in an inner membrane were obtained as described elsewhere ( Nekrasova et al., 2009a; Nekrasova et al., 2009b )."
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"The apparent dissociation constants of the Hetlaxin complexes with KcsA-Kv1.1 and KcsA-Kv1.3 were 800 nM and 59 nM, respectively [39] ."
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"The established K d values for GFP-OSK1 binding to KcsA-Kv1.1 and KcsA-Kv1.3 were 3.2 nM and 1.9 nM, respectively, while the K d values for RFP-AgTx2 binding to the same channels were 0.40 nM and 0.38[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"In comparison, R-AgTx2 binds KcsA-Kv1.1 and KcsA-Kv1.3 with K d values 3.4 nM [47] and 1.4 nM [40] respectively."
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"Recombinant RFP-tagged HgTX1 chimeras were shown to interact with KcsA-Kv1.1 and KcsA-Kv1.3 channels, however, the measured K d values depended on the tag position [71] ."
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"Chimeras KcsA-Kv1.1, KcsA-Kv1.2, KcsA-Kv1.3 and KcsA-Kv1.6 were shown to bind either 125 I-KTX (kaliotoxin) or 125 I-HgTX1(A19Y/Y37F) (hongotoxin 1 with two mutations) toxins with very high affinities[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Competition between R-AgTx2 and α-KTx (or TEA) for the binding to KcsA-Kv1.1 or KcsA-Kv1.3 channels was estimated by measuring average fluorescence signal intensity of R-AgTx2 per cell ( I av ) with a[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"These findings are also consistent with our findings that AETX-K blocks the Kv1.1 and KcsA pore with affinities of 1.6 pM and 0.3 nM ( xref ), respectively."
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"In competitive binding experiments, pharmacological profiles of well-known scorpion toxins, AgTx2, ChTX, KTX, OSK1, scyllatoxin (ScyTx), and margatoxin (MgTx), were investigated using KcsA-Kv1.1, KcsA[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Using fluorescent assay, it was found that the affinity of Hetlaxin to the external binding site of Kv1 channels decreases in the order KcsA-Kv1.3 ≫ KcsA-Kv1.1 ≫ KcsA-Kv1.6."
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"N-terminally labeled HgTX1, namely RFP-HgTX1, bound KcsA-Kv1.1 and KcsA-Kv1.3 channels with K d values of 35 and 15 nM, respectively, while these values for C-terminally labeled HgTX1-RFP were 19 and [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"It was found that A-AgTx2 effectively binds to spheroplasts expressing KcsA–Kv1.3 but does not stain spheroplasts presenting KcsA–Kv1.1 or KcsA–Kv1.6 ( xref A,B)."
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"Competition between fluorescent high-affinity blocker R-AgTx2 and tested α-KTx (or TEA) for the binding to KcsA-Kv1.1 or KcsA-Kv1.3 channels on the surface of spheroplasts is considered as an evidence[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Activity of recombinant α-KTx was confirmed by testing their ability to bind to KcsA-Kv1.1 and KcsA-Kv1.3 hybrid channels expressed in the inner membrane of E. coli spheroplasts."
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"eGFP-OSK1 and RFP-AgTx2 bind to KcsA-Kv1.1 with dissociation constants (mean ± S.E., n = 3) of 3.2 ± 1.1 and 0.4 ± 0.1 nM, respectively."
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"KcsA-Kv1.1 and KcsA-Kv1.3 hybrids retain affinity profile of the corresponding eukaryotic channels ( Kudryashova et al., 2013; Kuzmenkov et al., 2015b; Legros et al., 2000 ) and are able to specifical[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Considerable levels of KcsA–Kv1.1 and KcsA–Kv1.6 presentation in the plasma membrane as well as the ability of these channels to bind suitable pore blockers were confirmed in experiments with AgTx2-L3-GFP ( xref C)."
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"The results suggest that C-terminal labeling of HgTX1 was more favorable for binding of this peptide blocker to KcsA-Kv1.1 and, especially, to KcsA-Kv1.3 channels as compared with N-terminal position [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"In accordance with the previously reported properties [ xref ], AgTx2-L3-GFP intensely stained spheroplasts presenting KcsA–Kv1.1, KcsA–Kv1.3, or KcsA–Kv1.6 but not control spheroplasts ( xref C)."
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"Thus, HgTX1 N-terminally labeled with RFP [71] or Atto488 [59] demonstrated similar (decreased) binding affinities to the KcsA-Kv1.1 and KcsA-Kv1.3 channels, despite 25-fold difference in the molecula[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"AgTx2, KTx1, MgTx and HgTx are well-known high-affinity blockers of Kv1.1 and Kv1.3 ( http://kaliumdb.org ), and corresponding recombinant α-KTx obtained by us in this study displace readily R-AgTx2 f[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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