Intracellular domain of nicotinic acetylcholine receptor: the importance of being unfolded.

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Intracellular domain of nicotinic acetylcholine receptor: the importance of being unfolded. / Kukhtina, V; Kottwitz, Denise; Strauss, H; Heise, B; Chebotareva, N; Tsetlin, V; Hucho, F.

In: Journal of Neurochemistry, Vol. 97, No. Suppl 1, 2006, p. 63-67.

Research output: Contribution to journalArticle

Harvard

Kukhtina, V, Kottwitz, D, Strauss, H, Heise, B, Chebotareva, N, Tsetlin, V & Hucho, F 2006, 'Intracellular domain of nicotinic acetylcholine receptor: the importance of being unfolded.', Journal of Neurochemistry, vol. 97, no. Suppl 1, pp. 63-67. https://doi.org/10.1111/j.1471-4159.2005.03468.x

APA

Kukhtina, V., Kottwitz, D., Strauss, H., Heise, B., Chebotareva, N., Tsetlin, V., & Hucho, F. (2006). Intracellular domain of nicotinic acetylcholine receptor: the importance of being unfolded. Journal of Neurochemistry, 97(Suppl 1), 63-67. https://doi.org/10.1111/j.1471-4159.2005.03468.x

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MLA

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Author

Kukhtina, V ; Kottwitz, Denise ; Strauss, H ; Heise, B ; Chebotareva, N ; Tsetlin, V ; Hucho, F. / Intracellular domain of nicotinic acetylcholine receptor: the importance of being unfolded. In: Journal of Neurochemistry. 2006 ; Vol. 97, No. Suppl 1. pp. 63-67.

RIS

TY - JOUR

T1 - Intracellular domain of nicotinic acetylcholine receptor: the importance of being unfolded.

AU - Kukhtina, V

AU - Kottwitz, Denise

AU - Strauss, H

AU - Heise, B

AU - Chebotareva, N

AU - Tsetlin, V

AU - Hucho, F

PY - 2006

Y1 - 2006

N2 - Bioinformatics methods with subsequent verification by experimental data were applied to the structural investigation of the intracellular loop of the d-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.

AB - Bioinformatics methods with subsequent verification by experimental data were applied to the structural investigation of the intracellular loop of the d-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.

KW - eukaryotic linear motif

KW - intracellular domain

KW - limited proteolysis

KW - nicotinic acetylcholine receptor

KW - nuclear magnetic resonance

KW - secondary structure.

U2 - 10.1111/j.1471-4159.2005.03468.x

DO - 10.1111/j.1471-4159.2005.03468.x

M3 - Article

VL - 97

SP - 63

EP - 67

JO - Journal of Neurochemistry

JF - Journal of Neurochemistry

SN - 1471-4159

IS - Suppl 1

ER -