ABCB4 p.Gly187Glu

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PMID: 9521654 [PubMed] Kwan T et al: "Mutational analysis of the P-glycoprotein first intracellular loop and flanking transmembrane domains."
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194 Such mutants showed near wild-type transport Table 1: Summary of Mutations Identifieda TM2 IC1 TM3 EC2 TM4 Q128H R138H F159I S176P G187E R206L L210I Q128R Q139H V161E K177I A192T W208G T211P L134P Q139P H162R N179S F200L K209E V213A A136V Q139R T169I E180G F204S I214L Q145H R170L G181R I214T F147L L171P G183D S224P F148S T172P D184N E155G D174G E155K S176F a Summary of the mutations identified in the current screen together with their position within the predicted secondary structure of P-glycoprotein, with respect to the second (TM2), third (TM3), and fourth (TM4) predicted transmembrane domains together with the first intracellular (IC1) and second extracellular loop (EC2).
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ABCB4 p.Gly187Glu 9521654:194:131
status: NEW
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188 Group 1 comprised 17 mutants, including Q128R, L134P, F147L, F148S, F159I, V161E, H162R, T169I, R170L, L171P, T172P, G181R, G187E, W208G, K209E, I214L, and S224P.
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ABCB4 p.Gly187Glu 9521654:188:124
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207 This was particularly important in the case of Mdr3 mutants such as Q128R, L134P, V161E, R170L, L171P, G181R, G187E, and S224P that show complete loss of function in the three assays conducted.
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ABCB4 p.Gly187Glu 9521654:207:110
status: NEW
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