1kg0
From Proteopedia
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[[Image:1kg0.gif|left|200px]] | [[Image:1kg0.gif|left|200px]] | ||
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'''Structure of the Epstein-Barr Virus gp42 Protein Bound to the MHC class II Receptor HLA-DR1''' | '''Structure of the Epstein-Barr Virus gp42 Protein Bound to the MHC class II Receptor HLA-DR1''' | ||
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[[Category: Longnecker, R.]] | [[Category: Longnecker, R.]] | ||
[[Category: Mullen, M M.]] | [[Category: Mullen, M M.]] | ||
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- | [[Category: | + | [[Category: Membrane fusion]] |
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- | [[Category: | + | [[Category: Virus]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:42:05 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 19:42, 2 May 2008
Structure of the Epstein-Barr Virus gp42 Protein Bound to the MHC class II Receptor HLA-DR1
Overview
Epstein-Barr virus (EBV) causes infectious mononucleosis, establishes long-term latent infections, and is associated with a variety of human tumors. The EBV gp42 glycoprotein binds MHC class II molecules, playing a critical role in infection of B lymphocytes. EBV gp42 belongs to the C-type lectin superfamily, with homology to NK receptors of the immune system. We report the crystal structure of gp42 bound to the human MHC class II molecule HLA-DR1. The gp42 binds HLA-DR1 using a surface site that is distinct from the canonical lectin and NK receptor ligand binding sites. At the canonical ligand binding site, gp42 forms a large hydrophobic groove, which could interact with other ligands necessary for EBV entry, providing a mechanism for coupling MHC recognition and membrane fusion.
About this Structure
1KG0 is a Protein complex structure of sequences from Homo sapiens and Human herpesvirus 4. Full crystallographic information is available from OCA.
Reference
Structure of the Epstein-Barr virus gp42 protein bound to the MHC class II receptor HLA-DR1., Mullen MM, Haan KM, Longnecker R, Jardetzky TS, Mol Cell. 2002 Feb;9(2):375-85. PMID:11864610 Page seeded by OCA on Fri May 2 22:42:05 2008