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8T0O

Fab from mAb RB2AT_87

Summary for 8T0O
Entry DOI10.2210/pdb8t0o/pdb
DescriptorRB2AT_87 Fab Light chain, RB2AT_87 Fab Heavy chain, CHLORIDE ION, ... (4 entities in total)
Functional Keywordsfab fragment, monoclonal antibody, de novo protein, immune system
Biological sourceOryctolagus cuniculus
More
Total number of polymer chains2
Total formula weight46072.52
Authors
Kreutzer, A.G.,Malonis, R.J.,Lai, J.R.,Nowick, J.S. (deposition date: 2023-06-01, release date: 2024-03-27, Last modification date: 2024-10-23)
Primary citationKreutzer, A.G.,Malonis, R.J.,Parrocha, C.M.T.,Tong, K.,Guaglianone, G.,Nguyen, J.T.,Diab, M.N.,Lai, J.R.,Nowick, J.S.
Generation and Study of Antibodies against Two Triangular Trimers Derived from A beta.
Pept Sci (Hoboken), 116:-, 2024
Cited by
PubMed Abstract: Monoclonal antibodies (mAbs) that target the P-amyloid peptide (Aβ) are important Alzheimer's disease research tools and are now being used as Alzheimer's disease therapies. Conformation-specific mAbs that target oligomeric and fibrillar Aβ assemblies are of particular interest, as these assemblies are associated with Alzheimer's disease pathogenesis and progression. This paper reports the generation of rabbit mAbs against two different triangular trimers derived from Aβ. These antibodies are the first mAbs generated against Aβ oligomer mimics in which the high-resolution structures of the oligomers are known. We describe the isolation of the mAbs using single B-cell sorting of peripheral blood mononuclear cells (PBMCs) from immunized rabbits, the selectivity of the mAbs for the triangular trimers, the immunoreactivity of the mAbs with aggregated Aβ, and the immunoreactivity of the mAbs in brain tissue from the 5xFAD Alzheimer's disease mouse model. The characterization of these mAbs against structurally defined trimers derived from Aβ enhances understanding of antibody-amyloid recognition and may benefit the development of diagnostics and immunotherapies in Alzheimer's disease.
PubMed: 38644932
DOI: 10.1002/pep2.24333
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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