6lgw | pdb_00006lgw

Structure of Rabies virus glycoprotein in complex with neutralizing antibody 523-11 at acidic pH

spinqualitylabelsall models 6lgw, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6lgw is a 4 chain structure with sequence from Mus musculus and Rabies lyssavirus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9037Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GLYCO_RABVC Attaches the virus to host cellular receptor, inducing endocytosis of the virion. In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and cell membrane. There is convincing in vitro evidence that the muscular form of the nicotinic acetylcholine receptor (nAChR), the neuronal cell adhesion molecule (NCAM), and the p75 neurotrophin receptor (p75NTR) bind glycoprotein and thereby facilitate rabies virus entry into cells (By similarity). Publication Abstract from PubMed Rabies virus (RABV), the etiological agent for the lethal disease of rabies, is a deadly zoonotic pathogen. The RABV glycoprotein (RABV-G) is a key factor mediating virus entry and the major target of neutralizing antibodies. Here, we report the crystal structures of RABV-G solved in the free form at approximately pH-8.0 and in the complex form with a neutralizing antibody 523-11 at approximately pH-6.5, respectively. RABV-G has three domains, and the basic-to-acidic pH change results in large domain re-orientations and concomitant domain-linker re-constructions, switching it from a bent hairpin conformation into an extended conformation. During such low-pH-induced structural transitions, residues located in the domain-linker are found to play important roles in glycoprotein-mediated membrane fusion. Finally, the antibody interacts with RABV-G mainly through its heavy chain and binds to a bipartite conformational epitope in the viral protein for neutralization. These structures provide valuable information for vaccine and drug design. Structural Analysis of Rabies Virus Glycoprotein Reveals pH-Dependent Conformational Changes and Interactions with a Neutralizing Antibody.,Yang F, Lin S, Ye F, Yang J, Qi J, Chen Z, Lin X, Wang J, Yue D, Cheng Y, Chen Z, Chen H, You Y, Zhang Z, Yang Y, Yang M, Sun H, Li Y, Cao Y, Yang S, Wei Y, Gao GF, Lu G Cell Host Microbe. 2020 Jan 23. pii: S1931-3128(19)30641-9. doi:, 10.1016/j.chom.2019.12.012. PMID:32004500 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Antibody 3D structures Monoclonal Antibodies 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA