2 edition of Interactions between the transmembrane helices of the cystic fibrosis transmembrane conductance regulator (CFTR). found in the catalog.
Interactions between the transmembrane helices of the cystic fibrosis transmembrane conductance regulator (CFTR).
Mei Yee Choi
Written in English
Many membrane-based mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) involve introduction of a polar residue, which can lock helices together via a side chain-side chain interhelical non-native hydrogen bond to a neighboring wild type polar residue [i.e., Val 232-to-Asp (TM4) to Gln207 (TM3) (Therien, Grant & Deber, Nat. Struct. Biol., 2001]. We studied the Gln 207 H-bond "capture potential" by performing an Asp "walk" through TM4 in a series of TM3/4 helix-loop-helix (hairpin) constructs, assessing factors including the Asp position relative to the helix-helix interface, and side chain length and polarity. Diagnostic gel shift assays on SDS-PAGE were used to measure "open-closed" states of each hairpin. In related experiments, L346P and R347P mutants were investigated in a TM5/6 hairpin to determine why R347P inserts properly in the membrane, while L346P does not. The overall results help explain the molecular basis for aberrant CFTR function in CF-phenotypic TM domain mutants.
|The Physical Object|
|Number of Pages||106|
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