Crystal Structure of the Lymphocytic Choriomeningitis Virus Membrane Fusion Glycoprotein GP2 in its Postfusion ConformationCrystal Structure of the Lymphocytic Choriomeningitis Virus Membrane Fusion Glycoprotein GP2 in its Postfusion Conformation

Structural highlights

3mko is a 1 chain structure with sequence from Lymphocytic choriomeningitis mammarenavirus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GLYC_LYCVW The stable signal peptide (SSP) is cleaved and functions as a signal peptide. In addition, it is apparently retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of GP1 and GP2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion (By similarity). Glycoprotein G1 mediates virus attachment to host receptor alpha-dystroglycan DAG1. This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis (By similarity). Glycoprotein G2 is a viral fusion protein. Membrane fusion is mediated by conformational changes induced upon acidification in the endosome (Potential).

3mko, resolution 1.80Å

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