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Literature summary for 5.6.1.6 extracted from

  • Lewis, H.A.; Wang, C.; Zhao, X.; Hamuro, Y.; Conners, K.; Kearins, M.C.; Lu, F.; Sauder, J.M.; Molnar, K.S.; Coales, S.J.; Maloney, P.C.; Guggino, W.B.; Wetmore, D.R.; Weber, P.C.; Hunt, J.F.
    Structure and dynamics of NBD1 from CFTR characterized using crystallography and hydrogen/deuterium exchange mass spectrometry (2010), J. Mol. Biol., 396, 406-430.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli using as N-terminal His-tagged fusion protein Homo sapiens

Protein Variants

Protein Variants Comment Organism
DELTAF508 in-frame deletion without a phenylalanine residue at position 508 within nucleotide –binding domain 1: mass spectral measurements of backbone amide 1H/2H exchange rates in reveal that mutant DELTAF508 increases backbone dynamics at residues 509-511 and the adjacent protein segments but not elsewhere in NBD1. These measurements also confirm a high level of flexibility in the protein segments exhibiting variable conformations in the crystal structures Homo sapiens
DELTAF508/F409L/F4929S/F433L/G550E/R553Q/R555K/H667R mutant bearing an in-frame deletion without a phenylalanine residue at position 508 within nucleotide-binding domain 1 as well as several solubilizing mutations: Crystal structure refined at 2.55 A: The side chain of residue V510 in this loop is completely solvent exposed Homo sapiens
DELTAF508/F429S/F494N/Q637R mutant bearing an in-frame deletion without a phenylalanine residue at position 508 within nucleotide-binding domain 1 as well as several solubilizing mutations: Crystal structure refined at 2.3 A: The side chain of residue V510 in this loop is completely solvent exposed Homo sapiens
DELTAF508/F494N/Q637R mutant bearing an in-frame deletion without a phenylalanine residue at position 508 within nucleotide-binding domain 1 as well as several solubilizing mutations: Crystal structure refined at 2.05 A: The side chain of residue V510 in this loop is completely solvent exposed Homo sapiens
F409L/F4929S/F433L/G550E/R553Q/R555K/H667R mutant bearing no in-frame deletion of a phenylalanine residue at position 508 but with several solubilizing mutations: Crystal structure refined at 2.55 A: The side chain of residue V510 in this loop is buried Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P13569
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-

Purification (Commentary)

Purification (Comment) Organism
using Ni-NTA chromatography and gel filtration Homo sapiens

Synonyms

Synonyms Comment Organism
CFTR
-
Homo sapiens