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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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References listed in PDB file
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Key reference
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Title
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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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Authors
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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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Ref.
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Biopolymers, 1996,
40,
419-432.
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PubMed id
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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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Secondary reference #1
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Title
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Conformational requirements for molecular recognition of acetylcholine receptor main immunogenic region (mir) analogues by monoclonal anti-Mir antibody: a two-Dimensional nuclear magnetic resonance and molecular dynamics approach.
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Authors
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V.Tsikaris,
E.Detsikas,
M.Sakarellos-Daitsiotis,
C.Sakarellos,
E.Vatzaki,
S.J.Tzartos,
M.Marraud,
M.T.Cung.
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Ref.
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Biopolymers, 1993,
33,
1123-1134.
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PubMed id
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Secondary reference #2
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Title
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2d-Nmr and molecular dynamics analysis of the torpedo californica acetylcholine receptor alpha 67-76 fragment and of its [ala76]-Analogue.
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Authors
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M.T.Cung,
V.Tsikaris,
P.Demange,
I.Papadouli,
S.J.Tzartos,
C.Sakarellos,
M.Marraud.
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Ref.
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Pept Res, 1992,
5,
14-24.
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PubMed id
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Secondary reference #3
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Title
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Two-Dimensional 1h-Nmr study of antigen-Antibody interactions: binding of synthetic decapeptides to an anti-Acetylcholine receptor monoclonal antibody.
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Authors
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M.T.Cung,
P.Demange,
M.Marraud,
V.Tsikaris,
C.Sakarellos,
I.Papadouli,
A.Kokla,
S.J.Tzartos.
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Ref.
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Biopolymers, 1991,
31,
769-776.
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PubMed id
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Secondary reference #4
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Title
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Two-Dimensional 1h-Nmr study of synthetic peptides containing the main immunogenic region of the torpedo acetylcholine receptor.
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Authors
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M.T.Cung,
M.Marraud,
I.Hadjidakis,
E.Bairaktari,
C.Sakarellos,
A.Kokla,
S.Tzartos.
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Ref.
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Biopolymers, 1989,
28,
465-478.
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PubMed id
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Headers
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