Intracellular domain of nicotinic acetylcholine receptor: the importance of being unfolded.
(2006) In Journal of Neurochemistry 97(Suppl 1). p.63-67- Abstract
- 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... (More) - 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1137330
- author
- Kukhtina, V ; Kottwitz, Denise LU ; Strauss, H ; Heise, B ; Chebotareva, N ; Tsetlin, V and Hucho, F
- organization
- publishing date
- 2006
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- eukaryotic linear motif, intracellular domain, limited proteolysis, nicotinic acetylcholine receptor, nuclear magnetic resonance, secondary structure.
- in
- Journal of Neurochemistry
- volume
- 97
- issue
- Suppl 1
- pages
- 63 - 67
- publisher
- Wiley-Blackwell
- external identifiers
-
- scopus:33646839602
- pmid:16635251
- ISSN
- 1471-4159
- DOI
- 10.1111/j.1471-4159.2005.03468.x
- language
- English
- LU publication?
- yes
- id
- c818d47a-1f50-4c02-816a-aafb87f8fbd3 (old id 1137330)
- date added to LUP
- 2016-04-01 16:06:33
- date last changed
- 2022-04-15 02:11:09
@article{c818d47a-1f50-4c02-816a-aafb87f8fbd3,
abstract = {{Bioinformatics methods with subsequent verification by<br/><br>
experimental data were applied to the structural investigation<br/><br>
of the intracellular loop of the d-subunit of the nicotinic acetylcholine<br/><br>
receptor (nAChR). Three complementary methods<br/><br>
were used: prediction of secondary structure elements, prediction<br/><br>
of ordered/disordered protein regions and prediction of<br/><br>
short functional binding motifs. The output of five different<br/><br>
algorithms was used for the secondary structure construction.<br/><br>
Most of the intracellular domain is predicted to be unfolded.<br/><br>
The predictions correlate well with the experimental data of<br/><br>
limited proteolysis and NMR performed on the mostly monomeric<br/><br>
fraction of heterologously expressed Torpedo intracellular<br/><br>
domain protein. Twelve functional binding motifs within<br/><br>
the disordered regions of the nAChR intracellular domain are<br/><br>
predicted. Identification of proteins that interact with the<br/><br>
intracellular domain will provide a better understanding of<br/><br>
protein–protein interactions involved in nAChR assembly,<br/><br>
trafficking and clustering.}},
author = {{Kukhtina, V and Kottwitz, Denise and Strauss, H and Heise, B and Chebotareva, N and Tsetlin, V and Hucho, F}},
issn = {{1471-4159}},
keywords = {{eukaryotic linear motif; intracellular domain; limited
proteolysis; nicotinic acetylcholine receptor; nuclear
magnetic resonance; secondary structure.}},
language = {{eng}},
number = {{Suppl 1}},
pages = {{63--67}},
publisher = {{Wiley-Blackwell}},
series = {{Journal of Neurochemistry}},
title = {{Intracellular domain of nicotinic acetylcholine receptor: the importance of being unfolded.}},
url = {{http://dx.doi.org/10.1111/j.1471-4159.2005.03468.x}},
doi = {{10.1111/j.1471-4159.2005.03468.x}},
volume = {{97}},
year = {{2006}},
}