This data was extracted from Medline abstracts and full texts (when available) in an automated manner.
The table below describes different point mutations at a given position and provides links to other documents. The sentence(s) where the point mutations in KCNE3_HUMAN at position 72 were found are listed after the table.
Reference #1 (Melman YF et al.): V72A
- Recordings are from CHO cells (obtained as in Fig. 1 ) transfected with KvLQT1 cDNA with V72S KCNE3 (scale bar = 4000 pA) (a) ; V72C KCNE3 (scale bar = 4000 pA) (b) ; V72A KCNE3 (scale bar = 5000 pA) (c) ; V72I KCNE3 (scale bar = 4000 pA) (d) ; V72Y KCNE3 (scale bar = 9000 pA) (e) ; T58S minK (scale bar = 10 , 000 pA) (f) ; T58A minK (scale bar = 5000 pA) (g)
- Rise time was not determined (nd) for V72A KCNE3 because of unusual activation kinetics that did not saturate
- (V72S , n = 7 ; V72A , n = 7 ; V72Y , n = 7 ; V72I , n = 6 ; V72C , and n = 5.) That two sets of isosteric residues (threonine and valine , cysteine and serine) gave dramatically different currents solely with the introduction of a hydroxyl group suggests that this group has an important role in control KvLQT1 gating
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Reference #1 (Melman YF et al.): V72C
- The support for this hypothesis comes from V72C-KCNE3
- Recordings are from CHO cells (obtained as in Fig. 1 ) transfected with KvLQT1 cDNA with V72S KCNE3 (scale bar = 4000 pA) (a) ; V72C KCNE3 (scale bar = 4000 pA) (b) ; V72A KCNE3 (scale bar = 5000 pA) (c) ; V72I KCNE3 (scale bar = 4000 pA) (d) ; V72Y KCNE3 (scale bar = 9000 pA) (e) ; T58S minK (scale bar = 10 , 000 pA) (f) ; T58A minK (scale bar = 5000 pA) (g)
- (V72S , n = 7 ; V72A , n = 7 ; V72Y , n = 7 ; V72I , n = 6 ; V72C , and n = 5.) That two sets of isosteric residues (threonine and valine , cysteine and serine) gave dramatically different currents solely with the introduction of a hydroxyl group suggests that this group has an important role in control KvLQT1 gating
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Reference #1 (Melman YF et al.): V72I
- V72I-KCNE3 , a mutant that introduces a larger aliphatic residue , retained voltage-independent current and rapid activation characteristic of KCNE3 (Fig. 4 d)
- Recordings are from CHO cells (obtained as in Fig. 1 ) transfected with KvLQT1 cDNA with V72S KCNE3 (scale bar = 4000 pA) (a) ; V72C KCNE3 (scale bar = 4000 pA) (b) ; V72A KCNE3 (scale bar = 5000 pA) (c) ; V72I KCNE3 (scale bar = 4000 pA) (d) ; V72Y KCNE3 (scale bar = 9000 pA) (e) ; T58S minK (scale bar = 10 , 000 pA) (f) ; T58A minK (scale bar = 5000 pA) (g)
- (V72S , n = 7 ; V72A , n = 7 ; V72Y , n = 7 ; V72I , n = 6 ; V72C , and n = 5.) That two sets of isosteric residues (threonine and valine , cysteine and serine) gave dramatically different currents solely with the introduction of a hydroxyl group suggests that this group has an important role in control KvLQT1 gating
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Reference #1 (Melman YF et al.): V72S
- In substituting the hydroxylated residue serine into KCNE3 (V72S) , we observed slow voltage-dependent activation with sigmoidal kinetics and no voltage-independent constitutive current (Fig. 4 a)
- Recordings are from CHO cells (obtained as in Fig. 1 ) transfected with KvLQT1 cDNA with V72S KCNE3 (scale bar = 4000 pA) (a) ; V72C KCNE3 (scale bar = 4000 pA) (b) ; V72A KCNE3 (scale bar = 5000 pA) (c) ; V72I KCNE3 (scale bar = 4000 pA) (d) ; V72Y KCNE3 (scale bar = 9000 pA) (e) ; T58S minK (scale bar = 10 , 000 pA) (f) ; T58A minK (scale bar = 5000 pA) (g)
- (V72S , n = 7 ; V72A , n = 7 ; V72Y , n = 7 ; V72I , n = 6 ; V72C , and n = 5.) That two sets of isosteric residues (threonine and valine , cysteine and serine) gave dramatically different currents solely with the introduction of a hydroxyl group suggests that this group has an important role in control KvLQT1 gating
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Reference #1 (Melman YF et al.): V72T
- e , V72T KCNE3 (scale bar = 10 , 000 pA)
- g , T71F / V72T KCNE3 (scale bar = 700 pA)
- i , V72T / G73L KCNE3 (scale bar = 2000 pA)
- (T71F , n = 5 ; G73L , n = 5 ; T71F / V72T , n = 8 ; T71F / V72T , n = 8 ; and T71F / G73L , n = 6.) Fig. 1 , e-i , shows currents from KCNE3 with minK-substituted amino acids within the activation triplet
- All of the mutants containing the substitution V72T , either alone (Fig. 1 e) or in combination with another residue within the triplet (Fig. 1 , g and i) , abolished the usual KCNE3-mediated constitutive current and exhibited slow sigmoidal-type activation kinetics that resemble minK
- These two mutants contain a threonine located one turn up (N terminus) or one turn down the transmembrane alpha -helix of minK and , hence , would face the same direction as the threonine in V72T KCNE3
- This current was nearly identical to that produced by the V72T KCNE3 mutant , suggesting the need for a hydroxyl group at this position in producing slow sigmoidal voltage-dependent activation
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Reference #1 (Melman YF et al.): V72Y
- Recordings are from CHO cells (obtained as in Fig. 1 ) transfected with KvLQT1 cDNA with V72S KCNE3 (scale bar = 4000 pA) (a) ; V72C KCNE3 (scale bar = 4000 pA) (b) ; V72A KCNE3 (scale bar = 5000 pA) (c) ; V72I KCNE3 (scale bar = 4000 pA) (d) ; V72Y KCNE3 (scale bar = 9000 pA) (e) ; T58S minK (scale bar = 10 , 000 pA) (f) ; T58A minK (scale bar = 5000 pA) (g)
- (V72S , n = 7 ; V72A , n = 7 ; V72Y , n = 7 ; V72I , n = 6 ; V72C , and n = 5.) That two sets of isosteric residues (threonine and valine , cysteine and serine) gave dramatically different currents solely with the introduction of a hydroxyl group suggests that this group has an important role in control KvLQT1 gating
- Although V72Y KCNE3 has both rapid and slow activation , there is a significant voltage-independent component and no sigmoidal minK-like kinetics (Fig. 4 e) , suggesting that a hydrophobic group keeps the channel open in a voltage-independent manner and that precise spacing of the hydroxyl group is necessary to produce activation kinetics typical of I ks
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2005, KChannelDB.
cmbi.ru.nl), 17-Aug-2005