ABCMdb

PMID: 14685259

Lewis HA, Buchanan SG, Burley SK, Conners K, Dickey M, Dorwart M, Fowler R, Gao X, Guggino WB, Hendrickson WA, Hunt JF, Kearins MC, Lorimer D, Maloney PC, Post KW, Rajashankar KR, Rutter ME, Sauder JM, Shriver S, Thibodeau PH, Thomas PJ, Zhang M, Zhao X, Emtage S
Structure of nucleotide-binding domain 1 of the cystic fibrosis transmembrane conductance regulator.
EMBO J. 2004 Jan 28;23(2):282-93. Epub 2003 Dec 18., 2004-01-28 [PubMed]

Sentences

No. Mutations Sentence Comment

42 ABCC7 p.Lys464Ala A mutated version, K464A, which was expected to have reduced ATP binding, was also cloned and purified in the same manner and was used for ATP-binding measurements (see below). Login to comment 149 ABCC7 p.Lys464Ala ATP binding was significantly reduced by the K464A mutation, presumably because electrostatic interactions with the band g-phosphates of ATP (Figure 4A) are lost. Login to comment 201 ABCC7 p.Lys464Ala Wild type (K), K464A mutant (J), and ATP binding to the filters in the absence of protein (.) Login to comment 216 ABCC7 p.Gly551Asp ABCC7 p.Ala455Glu ABCC7 p.Ser549Arg ABCC7 p.Ser549Asn ABCC7 p.Arg560Thr ABCC7 p.Tyr569Asp ABCC7 p.Ile506Thr ABCC7 p.Gly480Cys ABCC7 p.Asp648Val ABCC7 p.Ala559Thr CF mutations in NBD1 The majority of sites of CF-causing missense mutations occur in NBD1, primarily in its a-subdomain, and the locations in the mNBD1 structure of the most common of these (A455E, G480C, I506T, DI507, DF508, S549N, S549R, G551D, A559T, R560T, Y569D, and D648V; Bobadilla et al, 2002) are shown in Figure 3D. Login to comment