5W3P
ANTIBODY C706 IN COMPLEX WTH BETA-AMYLOID PEPTIDE 1-16
Summary for 5W3P
Entry DOI | 10.2210/pdb5w3p/pdb |
Related | 3mcl |
Descriptor | Antibody C706 Fab LIGHT CHAIN, Antibody C706 Fab HEAVY CHAIN, Amyloid beta A4 protein, ... (6 entities in total) |
Functional Keywords | immune system |
Biological source | Mus musculus More |
Cellular location | Membrane; Single-pass type I membrane protein: P05067 |
Total number of polymer chains | 3 |
Total formula weight | 49074.28 |
Authors | Teplyakov, A.,Obmolova, G.,Gilliland, G.L. (deposition date: 2017-06-08, release date: 2017-09-20, Last modification date: 2024-10-16) |
Primary citation | Teplyakov, A.,Obmolova, G.,Gilliland, G.L. A coiled conformation of amyloid-beta recognized by antibody C706. Alzheimers Res Ther, 9:66-66, 2017 Cited by PubMed Abstract: β-Amyloid (Aβ) peptide is believed to play a pivotal role in the development of Alzheimer's disease. Passive immunization with anti-Aβ monoclonal antibodies may facilitate the clearance of Aβ in the brain and may thus prevent the downstream pathology. Antibodies targeting the immunodominant N-terminal epitope of Aβ and capable of binding both the plaques and soluble species have been most efficacious in animal models. Structural studies of such antibodies with bound Aβ peptides provided the basis for understanding the mechanisms of action and the differences in potency. To gain further insight into the structural determinants of antigen recognition and the preferential Aβ conformations, we determined the crystal structure of murine antibody C706 in complex with the N-terminal Aβ 1-16 peptide sequence. PubMed: 28830506DOI: 10.1186/s13195-017-0296-0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.92 Å) |
Structure validation
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