ABCC7 p.Gly241Asp
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PMID: 17516627
[PubMed]
Wehbi H et al: "Role of the extracellular loop in the folding of a CFTR transmembrane helical hairpin."
No.
Sentence
Comment
145
(iii) TM3/4 mutants G241D (38) and G241R (data not shown) migrate within 2% of WT.
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ABCC7 p.Gly241Asp 17516627:145:20
status: NEW
PMID: 15209503
[PubMed]
Choi MY et al: "Non-native interhelical hydrogen bonds in the cystic fibrosis transmembrane conductance regulator domain modulated by polar mutations."
No.
Sentence
Comment
162
Thus, for example, if one assumes that I231D in TM4 forms the closest contacts with Q207 in TM3, there are 10 residues ()2.7 turns of helix) from I231D for G241D.
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ABCC7 p.Gly241Asp 15209503:162:156
status: NEW165 Thus, the total vertical distance for the formation of an H-bond between Q207 in TM3 and G241D in TM4 will be about 15 Å (7.5 Å between the main chain carbon and the carboxamide in Q207 + 3 Å (average distance for H-bond formation) + 4.5 Å between the main chain carbon and the Asp carboxylate).
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ABCC7 p.Gly241Asp 15209503:165:89
status: NEW166 Using standard side chain torsional angles, models indicate that such H-bond formation is physically realistic between Q207 in TM3 and G241D in TM4.
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ABCC7 p.Gly241Asp 15209503:166:135
status: NEW180 Therefore, without Q237 (i.e., with Q237 mutated to Leu), the X f D mutants in TM4 become more open through regions encompassing A221D to G228D, and Q237D to G241D, and are ultimately unable to form an H-bond with Q207.
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ABCC7 p.Gly241Asp 15209503:180:158
status: NEW188 Nevertheless, for any A f D or G f D mutants (in this case, A221D, A223D, G226D, G228D, A234D, A238D, G239D, and G241D), only a single-base change is required, and therefore, it is possible these mutants represent potential phenotypic CF mutants, which have yet to be discovered.
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ABCC7 p.Gly241Asp 15209503:188:113
status: NEW