3FD4

Crystal Structure of Epstein-Barr virus gp42 protein

Summary for 3FD4

• Entry DOI: 10.2210/pdb3fd4/pdb
• Descriptor: Glycoprotein gp42 (2 entities in total)
• Functional Keywords: c type lectin, herpesvirus, virus entry, membrane fusion, host-virus interaction, lectin, membrane, transmembrane, viral protein
• Biological source: Human herpesvirus 4 (strain B95-8)
• Cellular location: Virion membrane : P03205
• Total number of polymer chains: 2
• Total formula weight: 43252.99

Authors

Kirschner, A.,Jardetzky, T. (deposition date: 2008-11-24, release date: 2009-06-23, Last modification date: 2024-10-30)

Primary citation

Kirschner, A.N.,Sorem, J.,Longnecker, R.,Jardetzky, T.S.
Structure of Epstein-Barr virus glycoprotein 42 suggests a mechanism for triggering receptor-activated virus entry.
Structure, 17:223-233, 2009

PubMed Abstract: Epstein-Barr virus requires glycoproteins gH/gL, gB, and gp42 to fuse its lipid envelope with B cells. Gp42 is a type II membrane protein consisting of a flexible N-terminal region, which binds gH/gL, and a C-terminal lectin-like domain that binds to the B-cell entry receptor human leukocyte antigen (HLA) class II. Gp42 triggers membrane fusion after HLA binding, a process that requires simultaneous binding to gH/gL and a functional hydrophobic pocket in the lectin domain adjacent to the HLA binding site. Here we present the structure of gp42 in its unbound form. Comparisons to the previously determined structure of a gp42:HLA complex reveals additional N-terminal residues forming part of the gH/gL binding site and structural changes in the receptor binding domain. Although the core of the lectin domain remains similar, significant shifts in two loops and an alpha helix bordering the essential hydrophobic pocket suggest a structural mechanism for triggering fusion.

PubMed: 19217393
DOI: 10.1016/j.str.2008.12.010

Experimental method

X-RAY DIFFRACTION (2.4 Å)