Sandbox Reserved 963: Difference between revisions
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Undo revision 2335725 by Kerim Secener (Talk) |
Undo revision 2335725 by Kerim Secener (Talk) |
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====Interactions with Glu3==== | ====Interactions with Glu3==== | ||
Hydrogen bond between the side chain of Glu3 and the main-chain amide of | Hydrogen bond between the side chain of Glu3 and the main-chain amide of Ser27(E)L. Additionally, there are potential salt bridges between the side chain of Glu3 and Nδ1/Nε2 atoms of His27(D)L. | ||
====Interactions with Phe4==== | ====Interactions with Phe4==== | ||
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===Comparison of unliganded and liganded WO2 Fab structures=== | ===Comparison of unliganded and liganded WO2 Fab structures=== | ||
Unliganded and liganded structures '''(Figure 4)''' superimpose very closely with an r.m.s.d. (root-mean-square deviation) of 0.3 Å on all Cα atoms (the r.m.s.d. is the measure of the average distance between the atoms of superimposed proteins[http://en.wikipedia.org/wiki/Root-mean-square_deviation]). Even the '''CDRs of liganded and unliganded states are barely distinguishable'''. Except for some small variations (<1 Å) around | Unliganded and liganded structures '''(Figure 4)''' superimpose very closely with an r.m.s.d. (root-mean-square deviation) of 0.3 Å on all Cα atoms (the r.m.s.d. is the measure of the average distance between the atoms of superimposed proteins[http://en.wikipedia.org/wiki/Root-mean-square_deviation]). Even the '''CDRs of liganded and unliganded states are barely distinguishable'''. Except for some small variations (<1 Å) around Ser27(E)L (L1), <scene name='60/604482/My_first_scene/11'>Lys33H (H1)</scene>, <scene name='60/604482/My_first_scene/16'>Asp54H (H2)</scene> and <scene name='60/604482/My_first_scene/17'>Glu100(C)H (H3)</scene>, there is no substantial change in the CDRs when Aβ binds with WO2. | ||
Moreover, thanks to temperature-factors analysis, it appears that CDR H1 is less flexible in the liganded structure.<ref>Amyloid-beta-anti-amyloid-beta complex structure reveals an extended conformation in the immunodominant B-cell epitope.,Miles LA, Wun KS, Crespi GA, Fodero-Tavoletti MT, Galatis D, Bagley CJ, Beyreuther K, Masters CL, Cappai R, McKinstry WJ, Barnham KJ, Parker MW J Mol Biol. 2008 Mar 14;377(1):181-92. Epub 2008 Jan 30. PMID:18237744</ref> | Moreover, thanks to temperature-factors analysis, it appears that CDR H1 is less flexible in the liganded structure.<ref>Amyloid-beta-anti-amyloid-beta complex structure reveals an extended conformation in the immunodominant B-cell epitope.,Miles LA, Wun KS, Crespi GA, Fodero-Tavoletti MT, Galatis D, Bagley CJ, Beyreuther K, Masters CL, Cappai R, McKinstry WJ, Barnham KJ, Parker MW J Mol Biol. 2008 Mar 14;377(1):181-92. Epub 2008 Jan 30. PMID:18237744</ref> | ||
[[Image:Fig. 1b.png|frame|'''Figure 4 :''' Representation of Aβ (shown as ball-and-stick) in the WO2 Fab variable domain CDRs after superimposition of their Cα atoms. The unliganded Form A is in yellow and the complex with Aβ<sub>1-16</sub> is in blue<ref>Amyloid-beta-anti-amyloid-beta complex structure reveals an extended conformation in the immunodominant B-cell epitope.,Miles LA, Wun KS, Crespi GA, Fodero-Tavoletti MT, Galatis D, Bagley CJ, Beyreuther K, Masters CL, Cappai R, McKinstry WJ, Barnham KJ, Parker MW J Mol Biol. 2008 Mar 14;377(1):181-92. Epub 2008 Jan 30. PMID:18237744</ref>]] | [[Image:Fig. 1b.png|frame|'''Figure 4 :''' Representation of Aβ (shown as ball-and-stick) in the WO2 Fab variable domain CDRs after superimposition of their Cα atoms. The unliganded Form A is in yellow and the complex with Aβ<sub>1-16</sub> is in blue<ref>Amyloid-beta-anti-amyloid-beta complex structure reveals an extended conformation in the immunodominant B-cell epitope.,Miles LA, Wun KS, Crespi GA, Fodero-Tavoletti MT, Galatis D, Bagley CJ, Beyreuther K, Masters CL, Cappai R, McKinstry WJ, Barnham KJ, Parker MW J Mol Biol. 2008 Mar 14;377(1):181-92. Epub 2008 Jan 30. PMID:18237744</ref>]] | ||
