3tby
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CRYSTAL STRUCTURE OF THE MURINE CLASS I MAJOR HISTOCOMPATIBILITY COMPLEX H-2DB IN COMPLEX WITH THE LCMV-DERIVED GP33 ALTERED PEPTIDE ligand (V3P, Y4F)
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Structural highlights
FunctionGLYC_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). See AlsoContents | ||||||||||||||||||
This page was last modified 10:28, 6 November 2024.