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PDBsum entry 1tor
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Transmembrane protein
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PDB id
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1tor
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PDB id:
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Transmembrane protein
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Title:
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Molecular dynamics simulation from 2d-nmr data of the free achr mir decapeptide and the antibody-bound [a76]mir analogue
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Structure:
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Acetylcholine receptor, main immunogenic region. Chain: a. Synonym: mir
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Source:
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Torpedo californica. Pacific electric ray. Organism_taxid: 7787
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NMR struc:
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5 models
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Authors:
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P.Orlewski,V.Tsikaris,C.Sakarellos,M.Sakarellos-Daistiotis,E.Vatzaki, S.J.Tzartos,M.Marraud,M.T.Cung
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Key ref:
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P.Orlewski
et al.
(1996).
Compared structures of the free nicotinic acetylcholine receptor main immunogenic region (MIR) decapeptide and the antibody-bound [A76]MIR analogue: a molecular dynamics simulation from two-dimensional NMR data.
Biopolymers,
40,
419-432.
PubMed id:
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Date:
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11-Oct-95
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Release date:
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08-Mar-96
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Headers
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References
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Biopolymers
40:419-432
(1996)
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PubMed id:
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Compared structures of the free nicotinic acetylcholine receptor main immunogenic region (MIR) decapeptide and the antibody-bound [A76]MIR analogue: a molecular dynamics simulation from two-dimensional NMR data.
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P.Orlewski,
M.Marraud,
M.T.Cung,
V.Tsikaris,
M.Sakarellos-Daitsiotis,
C.Sakarellos,
E.Vatzaki,
S.J.Tzartos.
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ABSTRACT
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Monoclonal antibodies against the main immunogenic region (MIR) of the muscle
acetylcholine receptor (AChR) are capable of inducing experimental myasthenia
gravis (MG) in animals. The epitope of these antibodies has been localized
between residues 67 and 76 of the AChR alpha-subunit. The conformation in
solution of the Torpedo californica MIR peptide and of its [A76] MIR analogue
have been analyzed using molecular modeling based on nmr interproton distances
and J-derived phi dihedral angles. Molecular dynamics simulations including
dimethyl-sulfoxide as explicit solvent have been carried out on the free MIR
peptide. Calculation of the structure of the [A76]MIR analogue bound to an
anti-MIR monoclonal antibody have been performed in the presence of water
molecules. A tightly folded structure appears for both peptides with alpha
beta-folded N-terminal N68-P-A-D71 sequence of type I in the free state and type
III in the mAb6-bound state. The C-terminal sequence is folded in two different
ways according to the result in the free and bound state of the peptides: two
overlapping beta/beta or beta/alpha turns result in a short helical sequence in
the free MIR peptide, whereas the bound analogue is folded by uncommon hydrogen
bond closing an 11-membered cycle. This structural evolution is essentially the
result of the reorientation of the hydrophobic side chains that are probably
directly involved in peptide--antibody recognition.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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T.K.Sixma,
and
A.B.Smit
(2003).
Acetylcholine binding protein (AChBP): a secreted glial protein that provides a high-resolution model for the extracellular domain of pentameric ligand-gated ion channels.
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Annu Rev Biophys Biomol Struct,
32,
311-334.
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K.Poulas,
E.Eliopoulos,
E.Vatzaki,
J.Navaza,
M.Kontou,
N.Oikonomakos,
K.R.Acharya,
and
S.J.Tzartos
(2001).
Crystal structure of Fab198, an efficient protector of the acetylcholine receptor against myasthenogenic antibodies.
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Eur J Biochem,
268,
3685-3693.
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PDB code:
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M.Kontou,
D.D.Leonidas,
E.H.Vatzaki,
P.Tsantili,
A.Mamalaki,
N.G.Oikonomakos,
K.R.Acharya,
and
S.J.Tzartos
(2000).
The crystal structure of the Fab fragment of a rat monoclonal antibody against the main immunogenic region of the human muscle acetylcholine receptor.
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Eur J Biochem,
267,
2389-2397.
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PDB code:
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J.Lindstrom,
X.Peng,
A.Kuryatov,
E.Lee,
R.Anand,
V.Gerzanich,
F.Wang,
G.Wells,
and
M.Nelson
(1998).
Molecular and antigenic structure of nicotinic acetylcholine receptors.
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Ann N Y Acad Sci,
841,
71-86.
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S.J.Tzartos,
T.Barkas,
M.T.Cung,
A.Mamalaki,
M.Marraud,
P.Orlewski,
D.Papanastasiou,
C.Sakarellos,
M.Sakarellos-Daitsiotis,
P.Tsantili,
and
V.Tsikaris
(1998).
Anatomy of the antigenic structure of a large membrane autoantigen, the muscle-type nicotinic acetylcholine receptor.
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Immunol Rev,
163,
89.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
