1tor: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1tor]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Torpedo_californica Torpedo 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TOR FirstGlance]. <br> | <table><tr><td colspan='2'>[[1tor]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Torpedo_californica Torpedo 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TOR FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tor OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1tor RCSB], [http://www.ebi.ac.uk/pdbsum/1tor PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tor OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1tor RCSB], [http://www.ebi.ac.uk/pdbsum/1tor PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/ACHA_TORCA ACHA_TORCA]] 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. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 18: | Line 20: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Torpedo californica]] | [[Category: Torpedo californica]] | ||
[[Category: Cung, M T | [[Category: Cung, M T]] | ||
[[Category: Marraud, M | [[Category: Marraud, M]] | ||
[[Category: Orlewski, P | [[Category: Orlewski, P]] | ||
[[Category: Sakarellos, C | [[Category: Sakarellos, C]] | ||
[[Category: Sakarellos-Daistiotis, M | [[Category: Sakarellos-Daistiotis, M]] | ||
[[Category: Tsikaris, V | [[Category: Tsikaris, V]] | ||
[[Category: Tzartos, S J | [[Category: Tzartos, S J]] | ||
[[Category: Vatzaki, E | [[Category: Vatzaki, E]] | ||
[[Category: Transmembrane protein]] | [[Category: Transmembrane protein]] | ||
Revision as of 17:54, 24 December 2014
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
Function[ACHA_TORCA] 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. Publication Abstract from PubMedMonoclonal 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. 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:9062066[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||