8AIC
X-ray structure of the receptor binding domain of Env glycoprotein of Simian Foamy virus
Summary for 8AIC
Entry DOI | 10.2210/pdb8aic/pdb |
Related | 8AEZ |
Descriptor | Envelope glycoprotein gp130, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
Functional Keywords | receptor binding domain, viral protein |
Biological source | Simian foamy virus |
Total number of polymer chains | 2 |
Total formula weight | 88565.44 |
Authors | Backovic, M.,Fernandez, I. (deposition date: 2022-07-26, release date: 2023-02-22, Last modification date: 2024-11-13) |
Primary citation | Fernandez, I.,Dynesen, L.T.,Coquin, Y.,Pederzoli, R.,Brun, D.,Haouz, A.,Gessain, A.,Rey, F.A.,Buseyne, F.,Backovic, M. The crystal structure of a simian Foamy Virus receptor binding domain provides clues about entry into host cells. Nat Commun, 14:1262-1262, 2023 Cited by PubMed Abstract: The surface envelope glycoprotein (Env) of all retroviruses mediates virus binding to cells and fusion of the viral and cellular membranes. A structure-function relationship for the HIV Env that belongs to the Orthoretrovirus subfamily has been well established. Structural information is however largely missing for the Env of Foamy viruses (FVs), the second retroviral subfamily. In this work we present the X-ray structure of the receptor binding domain (RBD) of a simian FV Env at 2.57 Å resolution, revealing two subdomains and an unprecedented fold. We have generated a model for the organization of the RBDs within the trimeric Env, which indicates that the upper subdomains form a cage-like structure at the apex of the Env, and identified residues K342, R343, R359 and R369 in the lower subdomain as key players for the interaction of the RBD and viral particles with heparan sulfate. PubMed: 36878926DOI: 10.1038/s41467-023-36923-0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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