ABCMdb

PMID: 20150177

Atwell S, Brouillette CG, Conners K, Emtage S, Gheyi T, Guggino WB, Hendle J, Hunt JF, Lewis HA, Lu F, Protasevich II, Rodgers LA, Romero R, Wasserman SR, Weber PC, Wetmore D, Zhang FF, Zhao X
Structures of a minimal human CFTR first nucleotide-binding domain as a monomer, head-to-tail homodimer, and pathogenic mutant.
Protein Eng Des Sel. 2010 May;23(5):375-84. Epub 2010 Feb 11., [PubMed]

Sentences

No. Mutations Sentence Comment

65 ABCC7 p.Phe429Ser ABCC7 p.Phe429Ser ABCC7 p.Phe494Asn ABCC7 p.Phe494Asn Human NBD1 proteins utilized Clone name Sequencea 2935c469 Ser-NBD1[387-646(D405-436)] 2935c472 Ser-NBD1[387-646(D405-436,DF508)] 2935c492 Ser-NBD1[375-646(D405-436)] 2935c382b Ser-NBD1[389-678(F429S,F494N,Q637R)] 2935c371c Ser-NBD1[389-678(F429S,F494N,Q637R, DF508)] a All of the NBD1 proteins start with a non-native serine preceding the NBD1 sequence. Login to comment 114 ABCC7 p.Phe429Ser ABCC7 p.Phe494Asn ABCC7 p.Gln637Arg Human NBD1 387-646(D405-436) is more stable and binds ATP tighter than non-truncated constructs Truncated and non-truncated NBD1 proteins were analyzed for their thermal unfolding properties: NBD1 387-646(D405-436) and NBD1 389-678[F429S,F494N,Q637R]. Login to comment 138 ABCC7 p.Phe429Ser ABCC7 p.Phe494Asn ABCC7 p.Gln637Arg (B) The same analysis was conducted with NBD1[389-678(F429S,F494N,Q637R)] proteins (2935c382 and 2935c371). Login to comment 207 ABCC7 p.Phe508Ala A similar analysis has been conducted comparing a human DF508 NBD1 with a human F508A NBD1 with different sets of solubilizing mutations (Lewis et al., 2005). Login to comment 226 ABCC7 p.Arg553Gln ABCC7 p.His667Arg ABCC7 p.Gly550Glu ABCC7 p.Arg555Lys ABCC7 p.Phe429Ser ABCC7 p.Phe409Leu ABCC7 p.Phe433Leu The 389-678(F409L, F429S, F433L, G550E, R553Q, R555K, H667R) (hNBD1-7a) structures are shown without (dark blue) and with the DF508 mutation (light blue) (H. Lewis, in preparation). Login to comment 249 ABCC7 p.Phe429Ser ABCC7 p.Phe409Leu ABCC7 p.Phe433Leu ABCC7 p.Phe494Asn Many of the solubilizing mutations developed for non-truncated NBD1 are in the RI or Q-loop cleft (F409L, F429S, F433L and F494N) and might function by reducing these interactions. Login to comment