6krv

Crystal structure of mouse IgG2b Fc complexed with B domain of Protein A

spinqualitylabelsall models 6krv, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6krv is a 4 chain structure with sequence from Mus musculus and Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.3Å Ligands: FUC, MAN, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function IGG2B_MOUSE Publication Abstract from PubMed Guillain-Barre syndrome, an autoimmune neuropathy characterized by acute limb weakness, is often preceded by Campylobacter jejuni infection. Molecular mimicry exists between the bacterial lipo-oligosaccharide and human ganglioside. Such C. jejuni infection induces production of immunoglobulin G1 (IgG1) autoantibodies against GM1 and causes complement-mediated motor nerve injury. For elucidating the molecular mechanisms linking autoantigen recognition and complement activation, we characterized the dynamic interactions of anti-GM1 IgG autoantibodies on ganglioside-incorporated membranes. Using high-speed atomic force microscopy, we found that the IgG molecules assemble into a hexameric ring structure on the membranes depending on their specific interactions with GM1. Complement component C1q was specifically recruited onto these IgG rings. The ring formation was inhibited by an IgG-binding domain of staphylococcal protein A bound at the cleft between the CH2 and CH3 domains. These data indicate that the IgG assembly is mediated through Fc-Fc interactions, which are promoted under on-membrane conditions due to restricted translational diffusion of IgG molecules. Reduction and alkylation of the hinge disulfide impaired IgG ring formation, presumably because of an increase in conformational entropic penalty. Our findings provide mechanistic insights into the molecular processes involved in Guillain-Barre syndrome and, more generally, into antigen-dependent interplay between antibodies and complement components on membranes. On-Membrane Dynamic Interplay between Anti-GM1 IgG Antibodies and Complement Component C1q.,Yanaka S, Yogo R, Watanabe H, Taniguchi Y, Satoh T, Komura N, Ando H, Yagi H, Yuki N, Uchihashi T, Kato K Int J Mol Sci. 2019 Dec 24;21(1). pii: ijms21010147. doi: 10.3390/ijms21010147. PMID:31878295 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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