PMID: 23658020

Wen PC, Verhalen B, Wilkens S, Mchaourab HS, Tajkhorshid E
On the origin of large flexibility of P-glycoprotein in the inward-facing state.
J Biol Chem. 2013 Jun 28;288(26):19211-20. doi: 10.1074/jbc.M113.450114. Epub 2013 May 8., [PubMed]
No. Mutations Sentence Comment
136 ABCB1 p.Gly185Val
ABCB1 p.Gly185Val 23658020:136:17
status: NEW
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Interestingly, a G185V mutation in human Pgp (equivalent to Gly-181 of mouse Pgp, a glycine that bends helix TM3, supplemental Fig. S6) is well studied and shown to improve the coupling between ATP hydrolysis and transport (72). Login to comment
137 ABCB1 p.Gly346Cys
ABCB1 p.Gly346Cys 23658020:137:17
status: NEW
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In addition, the G346C mutation in human Pgp (equivalent to Gly-342 of mouse Pgp, which causes a kink in helix TM6, supplemental Fig. S6) is FIGURE 4. Login to comment
147 ABCB1 p.Gly341Cys
ABCB1 p.Gly341Cys 23658020:147:263
status: NEW
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ABCB1 p.Gly360Cys
ABCB1 p.Gly360Cys 23658020:147:273
status: NEW
view ABCB1 p.Gly360Cys details
The suggested hinge role played by Gly-346 of human Pgp can also explain why the ATPase activity can only be significantly reduced by a mutation at this particular position but not elsewhere along the helix TM6 (73) even when other glycines in TM6 were targeted (G341C and G360C) (73). Login to comment