3M1C

Crystal structure of the conserved herpesvirus fusion regulator complex gH-gL

Summary for 3M1C

• Entry DOI: 10.2210/pdb3m1c/pdb
• Descriptor: Envelope glycoprotein H, Envelope glycoprotein L, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: glycoprotein h, glycoprotein l, gh/gl, envelope protein, herpes simplex virus, disulfide bond, glycoprotein, host cell membrane, host endosome, host membrane, membrane, transmembrane, virion, virus reference strain, viral protein
• Biological source: Human herpesvirus 2 (HHV-2); More
• Cellular location: Virion membrane ; Single-pass type I membrane protein : P89445; Virion membrane ; Peripheral membrane protein ; Extracellular side : P28278
• Total number of polymer chains: 2
• Total formula weight: 105835.13

Authors

Chowdary, T.K.,Heldwein, E.E. (deposition date: 2010-03-04, release date: 2010-07-07, Last modification date: 2024-11-06)

Primary citation

Chowdary, T.K.,Cairns, T.M.,Atanasiu, D.,Cohen, G.H.,Eisenberg, R.J.,Heldwein, E.E.
Crystal structure of the conserved herpesvirus fusion regulator complex gH-gL.
Nat.Struct.Mol.Biol., 17:882-888, 2010

PubMed Abstract: Herpesviruses, which cause many incurable diseases, infect cells by fusing viral and cellular membranes. Whereas most other enveloped viruses use a single viral catalyst called a fusogen, herpesviruses, inexplicably, require two conserved fusion-machinery components, gB and the heterodimer gH-gL, plus other nonconserved components. gB is a class III viral fusogen, but unlike other members of its class, it does not function alone. We determined the crystal structure of the gH ectodomain bound to gL from herpes simplex virus 2. gH-gL is an unusually tight complex with a unique architecture that, unexpectedly, does not resemble any known viral fusogen. Instead, we propose that gH-gL activates gB for fusion, possibly through direct binding. Formation of a gB-gH-gL complex is critical for fusion and is inhibited by a neutralizing antibody, making the gB-gH-gL interface a promising antiviral target.

PubMed: 20601960
DOI: 10.1038/nsmb.1837

Experimental method

X-RAY DIFFRACTION (3 Å)