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

Kukhtina, V ; Kottwitz, Denise LU ; Strauss, H ; Heise, B ; Chebotareva, N ; Tsetlin, V and Hucho, F (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:
author
; ; ; ; ; and
organization
publishing date
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
2021-10-06 04:27:39
@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},
  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},
}