Humanised 3d6 fab heavy chain. Chain: h. Engineered: yes. Humanised 3d6 fab light chain. Chain: l. Engineered: yes. Amyloid beta a4 protein. Chain: a. Fragment: unp residues 672-679.
Source:
Mus musculus. Mouse. Organism_taxid: 10090. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293. Synthetic: yes. Homo sapiens. Human.
Resolution:
2.00Å
R-factor:
0.174
R-free:
0.215
Authors:
L.A.Miles,G.A.N.Crespi,M.W.Parker
Key ref:
G.A.Crespi
et al.
(2014).
Crystallization and preliminary X-ray diffraction analysis of the Fab portion of the Alzheimer's disease immunotherapy candidate bapineuzumab complexed with amyloid-β.
Acta Crystallogr F Struct Biol Commun,
70,
374-377.
PubMed id: 24598931
DOI: 10.1107/S2053230X14001642
Crystallization and preliminary X-ray diffraction analysis of the Fab portion of the Alzheimer's disease immunotherapy candidate bapineuzumab complexed with amyloid-β.
G.A.Crespi,
D.B.Ascher,
M.W.Parker,
L.A.Miles.
ABSTRACT
Bapineuzumab (AAB-001) and its derivative (AAB-003) are humanized versions of
the anti-Aβ murine antibody 3D6 and are immunotherapy candidates in Alzheimer's
disease. The common Fab fragment of these immunotherapies has been expressed,
purified and crystallized in complex with β-amyloid peptides (residues 1-8 and
1-28). Diffraction data at high resolution were acquired from crystals of
Fab-Aβ8 (2.0 Å) and Fab-Aβ28 (2.2 Å) complexes at the Australian
Synchrotron. Both crystal forms belonged to the primitive orthorhombic space
group P21221.
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