2o5n

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(New page: 200px<br /><applet load="2o5n" size="350" color="white" frame="true" align="right" spinBox="true" caption="2o5n, resolution 2.400&Aring;" /> '''Crystal structure o...)
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==Overview==
==Overview==
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Mouse cytomegalovirus (MCMV), a ss-herpesvirus that establishes latent and, persistent infections in mice, is a valuable model for studying complex, virus-host interactions. MCMV encodes the m145 family of putative, immunoevasins with predicted MHC-I structure. Functions attributed to some, family members include downregulation of host MHC-I (m152) and NKG2D, ligands (m145, m152, m155) and interaction with inhibitory or activating, NK receptors (m157). We present the cellular, biochemical and structural, characterization of m153, which is a heavily glycosylated homodimer, that, does not require ss2m or peptide, and is expressed at the surface of, MCMV-infected cells. Its 2.4 A crystal structure confirms that this, compact molecule preserves an MHC-I-like fold and reveals a novel mode of, dimerization, confirmed by site-directed mutagenesis, and a distinctive, disulfide-stabilized extended amino terminus. The structure provides a, useful framework for comparative analysis of the divergent members of the, m145 family.
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Mouse cytomegalovirus (MCMV), a beta-herpesvirus that establishes latent and persistent infections in mice, is a valuable model for studying complex virus-host interactions. MCMV encodes the m145 family of putative immunoevasins with predicted major histocompatibility complex, class I (MHC-I) structure. Functions attributed to some family members include down-regulation of host MHC-I (m152) and NKG2D ligands (m145, m152, and m155) and interaction with inhibitory or activating NK receptors (m157). We present the cellular, biochemical, and structural characterization of m153, which is a heavily glycosylated homodimer, that does not require beta2m or peptide and is expressed at the surface of MCMV-infected cells. Its 2.4-A crystal structure confirms that this compact molecule preserves an MHC-I-like fold and reveals a novel mode of dimerization, confirmed by site-directed mutagenesis, and a distinctive disulfide-stabilized extended N terminus. The structure provides a useful framework for comparative analysis of the divergent members of the m145 family.
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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Cellular expression and crystal structure of the murine cytomegalovirus MHC-Iv glycoprotein, m153., Mans J, Natarajan K, Balbo A, Schuck P, Eikel D, Hess S, Robinson H, Simic H, Jonjic S, Tiemessen CT, Margulies DH, J Biol Chem. 2007 Sep 26;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17897947 17897947]
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Cellular expression and crystal structure of the murine cytomegalovirus major histocompatibility complex class I-like glycoprotein, m153., Mans J, Natarajan K, Balbo A, Schuck P, Eikel D, Hess S, Robinson H, Simic H, Jonjic S, Tiemessen CT, Margulies DH, J Biol Chem. 2007 Nov 30;282(48):35247-58. Epub 2007 Sep 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17897947 17897947]
[[Category: Murid herpesvirus 1]]
[[Category: Murid herpesvirus 1]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Mans, J.]]
[[Category: Mans, J.]]
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[[Category: Margulies, D.H.]]
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[[Category: Margulies, D H.]]
[[Category: Natarajan, K.]]
[[Category: Natarajan, K.]]
[[Category: Robinson, H.]]
[[Category: Robinson, H.]]
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[[Category: viral protein]]
[[Category: viral protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:22:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:14:43 2008''

Revision as of 16:14, 21 February 2008


2o5n, resolution 2.400Å

Drag the structure with the mouse to rotate

Crystal structure of a Viral Glycoprotein

Overview

Mouse cytomegalovirus (MCMV), a beta-herpesvirus that establishes latent and persistent infections in mice, is a valuable model for studying complex virus-host interactions. MCMV encodes the m145 family of putative immunoevasins with predicted major histocompatibility complex, class I (MHC-I) structure. Functions attributed to some family members include down-regulation of host MHC-I (m152) and NKG2D ligands (m145, m152, and m155) and interaction with inhibitory or activating NK receptors (m157). We present the cellular, biochemical, and structural characterization of m153, which is a heavily glycosylated homodimer, that does not require beta2m or peptide and is expressed at the surface of MCMV-infected cells. Its 2.4-A crystal structure confirms that this compact molecule preserves an MHC-I-like fold and reveals a novel mode of dimerization, confirmed by site-directed mutagenesis, and a distinctive disulfide-stabilized extended N terminus. The structure provides a useful framework for comparative analysis of the divergent members of the m145 family.

About this Structure

2O5N is a Protein complex structure of sequences from Murid herpesvirus 1 with as ligand. Full crystallographic information is available from OCA.

Reference

Cellular expression and crystal structure of the murine cytomegalovirus major histocompatibility complex class I-like glycoprotein, m153., Mans J, Natarajan K, Balbo A, Schuck P, Eikel D, Hess S, Robinson H, Simic H, Jonjic S, Tiemessen CT, Margulies DH, J Biol Chem. 2007 Nov 30;282(48):35247-58. Epub 2007 Sep 26. PMID:17897947

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