4XXD
| Crystal Structure of mid-region amyloid beta capture by solanezumab | Descriptor: | Amyloid-beta fragment, Fab Heavy Chain, Fab Light Chain | Authors: | Hermans, S.J, Crespi, G.A.N, Parker, M.W, Miles, L.A. | Deposit date: | 2015-01-30 | Release date: | 2015-04-29 | Last modified: | 2024-10-23 | Method: | X-RAY DIFFRACTION (2.41 Å) | Cite: | Molecular basis for mid-region amyloid-beta capture by leading Alzheimer's disease immunotherapies. Sci Rep, 5, 2015
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4OJF
| Humanised 3D6 Fab complexed to amyloid beta 1-8 | Descriptor: | Amyloid beta A4 protein, Humanised 3D6 Fab Heavy Chain, Humanised 3D6 Fab Light Chain | Authors: | Miles, L.A, Crespi, G.A.N, Parker, M.W. | Deposit date: | 2014-01-21 | Release date: | 2015-01-28 | Last modified: | 2024-10-16 | Method: | X-RAY DIFFRACTION (1.998 Å) | Cite: | Crystallization and preliminary X-ray diffraction analysis of the Fab portion of the Alzheimer's disease immunotherapy candidate bapineuzumab complexed with amyloid-beta ACTA CRYSTALLOGR.,SECT.F, 70, 2014
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4HIX
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3BAE
| Crystal structure of Fab WO2 bound to the N terminal domain of Amyloid beta peptide (1-28) | Descriptor: | Amyloid Beta Peptide, WO2 IgG2a Fab fragment Heavy Chain, WO2 IgG2a Fab fragment Light Chain Kappa | Authors: | Miles, L.A, Wun, K.S, Crespi, G.A, Parker, M.W. | Deposit date: | 2007-11-07 | Release date: | 2008-04-15 | Last modified: | 2023-11-01 | Method: | X-RAY DIFFRACTION (1.593 Å) | Cite: | Amyloid-beta-anti-amyloid-beta complex structure reveals an extended conformation in the immunodominant B-cell epitope. J.Mol.Biol., 377, 2008
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3BKC
| Crystal structure of anti-amyloid beta FAB WO2 (P21, FormB) | Descriptor: | SODIUM ION, WO2 IgG2a Fab fragment Heavy Chain, WO2 IgG2a Fab fragment Light Chain Kappa | Authors: | Miles, L.A, Wun, K.S, Crespi, G.A, Fodero-Tavoletti, M, Galatis, D, Bageley, C.J, Beyreuther, K, Masters, C.L, Cappai, R, McKinstry, W.J, Barnham, K.J, Parker, M.W. | Deposit date: | 2007-12-06 | Release date: | 2008-04-15 | Last modified: | 2024-10-30 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Amyloid-beta-anti-amyloid-beta complex structure reveals an extended conformation in the immunodominant B-cell epitope. J.Mol.Biol., 377, 2008
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3BKJ
| Crystal structure of Fab wo2 bound to the n terminal domain of amyloid beta peptide (1-16) | Descriptor: | Amyloid Beta Peptide, WO2 IgG2a Fab fragment Heavy Chain, WO2 IgG2a Fab fragment Light Chain Kappa | Authors: | Miles, L.A, Wun, K.S, Crespi, G.A, Fodero-Tavoletti, M, Galatis, D, Bageley, C.J, Beyreuther, K, Masters, C.L, Cappai, R, McKinstry, W.J, Barnham, K.J, Parker, M.W. | Deposit date: | 2007-12-06 | Release date: | 2008-04-15 | Last modified: | 2024-10-16 | Method: | X-RAY DIFFRACTION (1.59 Å) | Cite: | Amyloid-beta-anti-amyloid-beta complex structure reveals an extended conformation in the immunodominant B-cell epitope. J.Mol.Biol., 377, 2008
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3BKM
| Structure of anti-amyloid-beta Fab WO2 (Form A, P212121) | Descriptor: | SODIUM ION, WO2 IgG2a Fab fragment Heavy Chain, WO2 IgG2a Fab fragment Light Chain Kappa, ... | Authors: | Miles, L.A, Wun, K.S, Crespi, G.A, Fodero-Tavoletti, M, Galatis, D, Bageley, C.J, Beyreuther, K, Masters, C.L, Cappai, R, McKinstry, W.J, Barnham, K.J, Parker, M.W. | Deposit date: | 2007-12-07 | Release date: | 2008-04-15 | Last modified: | 2024-10-30 | Method: | X-RAY DIFFRACTION (1.6 Å) | Cite: | Amyloid-beta-anti-amyloid-beta complex structure reveals an extended conformation in the immunodominant B-cell epitope. J.Mol.Biol., 377, 2008
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3U0W
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8V5T
| Crystal structure of Alzheimers disease phospholipase D3 | Descriptor: | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 5'-3' exonuclease PLD3, GLYCEROL, ... | Authors: | Ishii, K, Hermans, S.J, Nero, T.L, Gorman, M.A, Parker, M.W. | Deposit date: | 2023-12-01 | Release date: | 2024-10-09 | Method: | X-RAY DIFFRACTION (2.3 Å) | Cite: | Crystal structure of Alzheimer's disease phospholipase D3 provides a molecular basis for understanding its normal and pathological functions. Febs J., 2024
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6D48
| Cell Surface Receptor | Descriptor: | Myeloid cell surface antigen CD33 | Authors: | Hermans, S.J, Miles, L.A, Parker, M.W. | Deposit date: | 2018-04-17 | Release date: | 2019-04-17 | Last modified: | 2024-10-30 | Method: | X-RAY DIFFRACTION (1.776 Å) | Cite: | Small Molecule Binding to Alzheimer Risk Factor CD33 Promotes A beta Phagocytosis. Iscience, 19, 2019
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6D49
| Cell Surface Receptor in Complex with Ligand at 1.80-A Resolution | Descriptor: | 2-aminoethyl 5-{[(4-cyclohexyl-1H-1,2,3-triazol-1-yl)acetyl]amino}-3,5,9-trideoxy-9-[(4-hydroxy-3,5-dimethylbenzene-1-carbonyl)amino]-D-glycero-alpha-D-galacto-non-2-ulopyranonosyl-(2->6)-beta-D-galactopyranosyl-(1->4)-beta-D-glucopyranoside, GLYCEROL, Myeloid cell surface antigen CD33 | Authors: | Hermans, S.J, Miles, L.A, Parker, M.W. | Deposit date: | 2018-04-17 | Release date: | 2019-04-17 | Last modified: | 2024-10-30 | Method: | X-RAY DIFFRACTION (1.801 Å) | Cite: | Small Molecule Binding to Alzheimer Risk Factor CD33 Promotes A beta Phagocytosis. Iscience, 19, 2019
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6D4A
| Cell Surface Receptor with Bound Ligand at 1.75-A Resolution | Descriptor: | 2-aminoethyl 5-{[(4-cyclohexyl-1H-1,2,3-triazol-1-yl)acetyl]amino}-3,5,9-trideoxy-9-[(4-hydroxy-3,5-dimethylbenzene-1-carbonyl)amino]-D-glycero-alpha-D-galacto-non-2-ulopyranonosyl-(2->6)-beta-D-galactopyranosyl-(1->4)-beta-D-glucopyranoside, GLYCEROL, Myeloid cell surface antigen CD33 | Authors: | Hermans, S.J, Miles, L.A, Parker, M.W. | Deposit date: | 2018-04-17 | Release date: | 2019-04-17 | Last modified: | 2024-10-23 | Method: | X-RAY DIFFRACTION (1.751 Å) | Cite: | Small Molecule Binding to Alzheimer Risk Factor CD33 Promotes A beta Phagocytosis. Iscience, 19, 2019
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5BUO
| A receptor molecule | Descriptor: | 2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose, ACETATE ION, Amyloid beta A4 protein, ... | Authors: | Gao, C, Crespi, G.A.N, Gorman, M.A, Nero, T.L, Parker, M.W, Miles, L.A. | Deposit date: | 2015-06-04 | Release date: | 2016-07-13 | Last modified: | 2023-09-27 | Method: | X-RAY DIFFRACTION (2.31 Å) | Cite: | NULL To Be Published
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