3MOQ
Amyloid beta(18-41) peptide fusion with new antigen receptor variable domain from sharks
Summary for 3MOQ
| Entry DOI | 10.2210/pdb3moq/pdb |
| Descriptor | New antigen receptor variable domain,P3(40) peptide from Amyloid beta A4 protein,New antigen receptor variable domain (2 entities in total) |
| Functional Keywords | ab-ignar, ab-12y-2, receptor, amyloid, glycoprotein, membrane, protease inhibitor, serine protease inhibitor, transmembrane, amyloid beta fusion with ignar, chimera of immune system and amyloid peptide, immune system, neuropeptide |
| Biological source | Orectolobus maculatus (spotted wobbegong) More |
| Total number of polymer chains | 4 |
| Total formula weight | 53864.52 |
| Authors | Streltsov, V.A. (deposition date: 2010-04-23, release date: 2011-02-16, Last modification date: 2024-10-30) |
| Primary citation | Streltsov, V.A.,Varghese, J.N.,Masters, C.L.,Nuttall, S.D. Crystal Structure of the Amyloid-{beta} p3 Fragment Provides a Model for Oligomer Formation in Alzheimer's Disease J.Neurosci., 31:1419-1426, 2011 Cited by PubMed Abstract: Alzheimer's disease is a progressive neurodegenerative disorder associated with the presence of amyloid-β (Aβ) peptide fibrillar plaques in the brain. However, current evidence suggests that soluble nonfibrillar Aβ oligomers may be the major drivers of Aβ-mediated synaptic dysfunction. Structural information on these Aβ species has been very limited because of their noncrystalline and unstable nature. Here, we describe a crystal structure of amylogenic residues 18-41 of the Aβ peptide (equivalent to the p3 α/γ-secretase fragment of amyloid precursor protein) presented within the CDR3 loop region of a shark Ig new antigen receptor (IgNAR) single variable domain antibody. The predominant oligomeric species is a tightly associated Aβ dimer, with paired dimers forming a tetramer in the crystal caged within four IgNAR domains, preventing uncontrolled amyloid formation. Our structure correlates with independently observed features of small nonfibrillar Aβ oligomers and reveals conserved elements consistent with residues and motifs predicted as critical in Aβ folding and oligomerization, thus potentially providing a model system for nonfibrillar oligomer formation in Alzheimer's disease. PubMed: 21273426DOI: 10.1523/JNEUROSCI.4259-10.2011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.054 Å) |
Structure validation
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