ABCC7 p.Asn1148Ala
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PMID: 22160394
[PubMed]
Cui G et al: "Differential contribution of TM6 and TM12 to the pore of CFTR identified by three sulfonylurea-based blockers."
No.
Sentence
Comment
150
Surprisingly, nine mutations of TM12, including N1138A, M1140A, T1142A, V1147A, N1148A, S1149A, S1150A, I1151A, and D1152A, exhibited significantly altered block by Glyb; the pattern was not consistent with either α-helix or β-strand secondary structure along the full length of the region studied.
X
ABCC7 p.Asn1148Ala 22160394:150:80
status: NEW163 Effects on time-dependent block by mutations R334A and K335A Fractional block by Glip200 μM V1153A D1152A I1151A S1150A S1149A N1148A V1147A A1146S W1145A Q1144A L1143A T1142A S1141A M1140A I1139A N1138A M1137A A1136S L1135A T1134A WT 0 0.2 0.4 0.6 0.8 * ** ** ** ** ** ** * V1153A D1152A I1151A S1150A S1149A N1148A V1147A A1146S W1145A Q1144A L1143A T1142A S1141A M1140A I1139A N1138A M1137A A1136S L1135A T1134A WT 0 0.2 0.4 0.6 0.8 1.0 * * * * * ** ** ** ** Fractional block by Glyb50 μM Fig. 4 Alanine-scanning in TM12 to identify amino acids that interact with Glyb and Glip.
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ABCC7 p.Asn1148Ala 22160394:163:133
status: NEWX
ABCC7 p.Asn1148Ala 22160394:163:316
status: NEW180 Surprisingly, several mutations in TM12 Q1144A, V1147A, N1148A, S1149A, S1150A, and I1151A affected the voltage-dependence of block by Glyb (Fig. 8b).
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ABCC7 p.Asn1148Ala 22160394:180:56
status: NEW