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Intracellular domain of nicotinic acetylcholine receptor: the importance of being unfolded
Author(s) -
Kukhtina V.,
Kottwitz D.,
Strauss H.,
Heise B.,
Chebotareva N.,
Tsetlin V.,
Hucho F.
Publication year - 2006
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2005.03468.x
Subject(s) - intracellular , torpedo , nicotinic acetylcholine receptor , protein subunit , acetylcholine receptor , protein structure , biology , biophysics , microbiology and biotechnology , chemistry , biochemistry , computational biology , receptor , gene
Bioinformatics methods with subsequent verification by experimental data were applied to the structural investigation of the intracellular loop of the δ‐subunit of the nicotinic acetylcholine receptor (nAChR). Three complementary methods were used: prediction of secondary structure elements, prediction of ordered/disordered protein regions and prediction of short functional binding motifs. The output of five different algorithms was used for the secondary structure construction. Most of the intracellular domain is predicted to be unfolded. The predictions correlate well with the experimental data of limited proteolysis and NMR performed on the mostly monomeric fraction of heterologously expressed Torpedo intracellular domain protein. Twelve functional binding motifs within the disordered regions of the nAChR intracellular domain are predicted. Identification of proteins that interact with the intracellular domain will provide a better understanding of protein–protein interactions involved in nAChR assembly, trafficking and clustering.