ABCMdb

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 ABCC7 p.Glu1371Ser 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 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 ABCC7 p.Glu1371Ser 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