1kg0

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(New page: 200px<br /> <applet load="1kg0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kg0, resolution 2.65&Aring;" /> '''Structure of the Ep...)
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<applet load="1kg0" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1kg0, resolution 2.65&Aring;" />
caption="1kg0, resolution 2.65&Aring;" />
'''Structure of the Epstein-Barr Virus gp42 Protein Bound to the MHC class II Receptor HLA-DR1'''<br />
'''Structure of the Epstein-Barr Virus gp42 Protein Bound to the MHC class II Receptor HLA-DR1'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1KG0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KG0 OCA].
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1KG0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KG0 OCA].
==Reference==
==Reference==
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[[Category: Human herpesvirus 4]]
[[Category: Human herpesvirus 4]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Haan, K.M.]]
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[[Category: Haan, K M.]]
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[[Category: Jardetzky, T.S.]]
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[[Category: Jardetzky, T S.]]
[[Category: Longnecker, R.]]
[[Category: Longnecker, R.]]
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[[Category: Mullen, M.M.]]
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[[Category: Mullen, M M.]]
[[Category: c-type lectin domain]]
[[Category: c-type lectin domain]]
[[Category: membrane fusion]]
[[Category: membrane fusion]]
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[[Category: virus]]
[[Category: virus]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:50:39 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:33:44 2008''

Revision as of 11:33, 21 February 2008


1kg0, resolution 2.65Å

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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

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