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1XMI The alpha helices in pink and beta sheets shown in yellow make up the secondary structures. Regions that are without secondary structures are white.This strucutre contains 37% helical (15 helices; 108 residues) and 19% beta sheets (11 strands). With a crystal diffracting to a resolution of 2.3 Å were
obtained for hNBD1-ΔF508, which contains seven mutations (F409L,
F429S, F433L, G550E, R553Q, R555K, H667R) in addition to the
deletion of Phe-508.
Citation 1XMI (PDB) |
1XMI The alpha helices in pink and beta sheets shown in yellow make up the secondary structures. Regions that are without secondary structures are white. Deletion of Phe-508 is accommodated through a simple shortening of the loop connecting α-helices 3 and 4 in the ABCα subdomain. deletion causes Gly-509 to move into the position occupied by Phe-508, resulting in a >90° rotation of the side chain of Val-510 as it moves into the center of the interhelical loop as well as reorganization of the backbone of residues 509-510. The changes result in significant change in both the topography and chemical properties of the surface Impact of the delta-F508 Mutation in First Nucleotide-binding Domain of Human Cystic Fibrosis Transmembrane Conductance Regulator on Domain Folding and Structure 1XMI (PDB)
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