PMID: 21461971

Krasilnikov OV, Sabirov RZ, Okada Y
ATP hydrolysis-dependent asymmetry of the conformation of CFTR channel pore.
J Physiol Sci. 2011 Jul;61(4):267-78. doi: 10.1007/s12576-011-0144-0. Epub 2011 Apr 3., [PubMed]
Sentences
No. Mutations Sentence Comment
31 ABCC7 p.Lys1250Ala
X
ABCC7 p.Lys1250Ala 21461971:31:109
status: NEW
view ABCC7 p.Lys1250Ala details
ABCC7 p.Glu1371Ser
X
ABCC7 p.Glu1371Ser 21461971:31:119
status: NEW
view ABCC7 p.Glu1371Ser details
This locked-open phenotype is also observed when the ATPase activity of NBD2 is abolished by the mutation of K1250A or E1371S [10, 23, 39]. Login to comment
201 ABCC7 p.Arg334Cys
X
ABCC7 p.Arg334Cys 21461971:201:71
status: NEW
view ABCC7 p.Arg334Cys details
In contrast, real time measurements of covalent modification of single R334C-CFTR channels by [2-(trimethylammonium)ethyl]methanethiosulfonate indicated that a single CFTR polypeptide forms a CFTR channel with a single pore [25]. Login to comment
225 ABCC7 p.Lys1250Ala
X
ABCC7 p.Lys1250Ala 21461971:225:108
status: NEW
view ABCC7 p.Lys1250Ala details
ABCC7 p.Glu1371Ser
X
ABCC7 p.Glu1371Ser 21461971:225:119
status: NEW
view ABCC7 p.Glu1371Ser details
An intriguing question as to whether the mutation at the site essential for ATP hydrolysis in NBD2 (such as K1250A and E1371S) causes a similar conformational change remains for future studies. Login to comment