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New page: left|200px<br /> <applet load="1tor" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tor" /> '''MOLECULAR DYNAMICS SIMULATION FROM 2D-NMR D...
 
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[[Image:1tor.gif|left|200px]]<br />
<applet load="1tor" size="450" color="white" frame="true" align="right" spinBox="true"
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'''MOLECULAR DYNAMICS SIMULATION FROM 2D-NMR DATA OF THE FREE ACHR MIR DECAPEPTIDE AND THE ANTIBODY-BOUND [A76]MIR ANALOGUE'''<br />


==Overview==
==MOLECULAR DYNAMICS SIMULATION FROM 2D-NMR DATA OF THE FREE ACHR MIR DECAPEPTIDE AND THE ANTIBODY-BOUND [A76]MIR ANALOGUE==
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.
<StructureSection load='1tor' size='340' side='right'caption='[[1tor]]' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1tor]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tetronarce_californica Tetronarce californica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TOR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TOR FirstGlance]. <br>
1TOR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Torpedo_californica Torpedo californica]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TOR OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
 
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tor OCA], [https://pdbe.org/1tor PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tor RCSB], [https://www.ebi.ac.uk/pdbsum/1tor PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tor ProSAT]</span></td></tr>
==Reference==
</table>
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., Orlewski P, Marraud M, Cung MT, Tsikaris V, Sakarellos-Daitsiotis M, Sakarellos C, Vatzaki E, Tzartos SJ, Biopolymers. 1996;40(5):419-32. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9062066 9062066]
== Function ==
[[Category: Single protein]]
[https://www.uniprot.org/uniprot/ACHA_TETCF ACHA_TETCF] After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
[[Category: Torpedo californica]]
__TOC__
[[Category: Cung, M.T.]]
</StructureSection>
[[Category: Marraud, M.]]
[[Category: Large Structures]]
[[Category: Orlewski, P.]]
[[Category: Tetronarce californica]]
[[Category: Sakarellos, C.]]
[[Category: Cung MT]]
[[Category: Sakarellos-Daistiotis, M.]]
[[Category: Marraud M]]
[[Category: Tsikaris, V.]]
[[Category: Orlewski P]]
[[Category: Tzartos, S.J.]]
[[Category: Sakarellos C]]
[[Category: Vatzaki, E.]]
[[Category: Sakarellos-Daistiotis M]]
[[Category: transmembrane protein]]
[[Category: Tsikaris V]]
 
[[Category: Tzartos SJ]]
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:42:59 2007''
[[Category: Vatzaki E]]

Latest revision as of 09:35, 1 May 2024

MOLECULAR DYNAMICS SIMULATION FROM 2D-NMR DATA OF THE FREE ACHR MIR DECAPEPTIDE AND THE ANTIBODY-BOUND [A76]MIR ANALOGUEMOLECULAR DYNAMICS SIMULATION FROM 2D-NMR DATA OF THE FREE ACHR MIR DECAPEPTIDE AND THE ANTIBODY-BOUND [A76]MIR ANALOGUE

Structural highlights

1tor is a 1 chain structure with sequence from Tetronarce californica. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ACHA_TETCF After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.

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