Sandbox Reserved 963: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 104: | Line 104: | ||
Residues of the light chain closely contacting Aβ residues include <scene name='60/604482/His_27/2'>His27(D)L</scene>, <scene name='60/604482/Ser27/2'> Ser27(E)L </scene> and <scene name='60/604482/My_first_scene/18'>Tyr32L</scene> from light-chain CDR 1 (L1) and <scene name='60/604482/My_first_scene/7'>Ser92L, Leu93L, Val94L and Leu96L from L3</scene>. | Residues of the light chain closely contacting Aβ residues include <scene name='60/604482/His_27/2'>His27(D)L</scene>, <scene name='60/604482/Ser27/2'> Ser27(E)L </scene> and <scene name='60/604482/My_first_scene/18'>Tyr32L</scene> from light-chain CDR 1 (L1) and <scene name='60/604482/My_first_scene/7'>Ser92L, Leu93L, Val94L and Leu96L from L3</scene>. | ||
All residues from Phe4 to Ser8, except Asp7, make close contact with the WO2 heavy-chain CDRs. Close contacting interface residues include <scene name='60/604482/My_first_scene/8'>His50H, Tyr52H, Asp54H and | All residues from Phe4 to Ser8, except Asp7, make close contact with the WO2 heavy-chain CDRs. Close contacting interface residues include <scene name='60/604482/My_first_scene/8'>His50H, Tyr52H, Asp54H and Asp56H from H2</scene> and <scene name='60/604482/My_first_scene/9'>Tyr100(B)H and Asn100(E)H from H3</scene>. | ||
Also, we observe no contact between Aβ and the L2 or H1 CDRs of WO2 and there is no evidence in the structure of any water-mediated contacts between WO2 and Aβ.<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> | Also, we observe no contact between Aβ and the L2 or H1 CDRs of WO2 and there is no evidence in the structure of any water-mediated contacts between WO2 and Aβ.<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> | ||
| Line 127: | Line 127: | ||
*The side chain of Arg5 forms : | *The side chain of Arg5 forms : | ||
**Two hydrogen bonds with the carboxylate group of <scene name='60/604482/Asp54h/1'> Asp54H </scene> | **Two hydrogen bonds with the carboxylate group of <scene name='60/604482/Asp54h/1'> Asp54H </scene> | ||
**One hydrogen bond with the side chain of | **One hydrogen bond with the side chain of Asp56H | ||
*The main chain of Arg5 interacts with the side-chain hydroxyl (OH) of Tyr52H | *The main chain of Arg5 interacts with the side-chain hydroxyl (OH) of Tyr52H | ||
