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Functional dissection of the R domain of cystic fibrosis transmembrane conductance regulator 1
Author(s) -
Tasch Jason E.,
Zerhusen Bryan,
Zhao Jiying,
Ma Jianjie,
Davis Pamela B.
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00086-1
Subject(s) - cystic fibrosis transmembrane conductance regulator , block (permutation group theory) , domain (mathematical analysis) , regulator , chemistry , transmembrane domain , biophysics , transmembrane protein , conductance , amino acid , crystallography , biology , biochemistry , gene , physics , receptor , combinatorics , mathematics , condensed matter physics , mathematical analysis
Exogenously expressed unphosphorylated sub‐domains of the R domain block CFTR Cl − channels in the planar lipid bilayer, though the block differs from block with full length R domain. Full length R domain peptide (aa 588–855) blocks CFTR Cl − channels quickly, completely and permanently [1]. Two sub‐domains, RD1RD2 (aa 588–805) and RD2TM (aa 672–855), also inhibit CFTR Cl − channels, but the block takes longer to effect and is not complete. Shorter sequences, RD1 (aa 588–746) and RD2 (aa 672–805), fail to effect any block. These data suggest that either the amino‐terminal or carboxy‐terminal portions of the R domain protein or its stabilized secondary structure are critical to functional regulation.