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| [[Image:2uwi.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2uwi| PDB=2uwi | SCENE= }} | | {{STRUCTURE_2uwi| PDB=2uwi | SCENE= }} |
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| '''STRUCTURE OF CRME, A POXVIRUS TNF RECEPTOR'''
| | ===STRUCTURE OF CRME, A POXVIRUS TNF RECEPTOR=== |
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| ==Overview==
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| Vaccinia virus (VACV), the smallpox vaccine, encodes many proteins that subvert the host immune response. One of these, cytokine response modifier E (CrmE), is secreted by infected cells and protects these cells from apoptotic challenge by tumour necrosis factor alpha (TNFalpha). We have expressed recombinant CrmE from VACV strain Lister in Escherichia coli, shown that the purified protein is monomeric in solution and competent to bind TNFalpha, and solved the structure to 2.0 A resolution. This is the first structure of a virus-encoded tumour necrosis factor receptor (TNFR). CrmE shares significant sequence similarity with mammalian type 2 TNF receptors (TNFSFR1B, p75; TNFR type 2). The structure confirms that CrmE adopts the canonical TNFR fold but only one of the two "ligand-binding" loops of TNFRSF1A is conserved in CrmE, suggesting a mechanism for the higher affinity of poxvirus TNFRs for TNFalpha over lymphotoxin-alpha. The roles of dimerisation and pre-ligand-assembly domains (PLADs) in poxvirus and mammalian TNFR activity are discussed.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17681535}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17681535 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17681535}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Receptor immunomodulator]] | | [[Category: Receptor immunomodulator]] |
| [[Category: Tnf alpha receptor]] | | [[Category: Tnf alpha receptor]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:39:52 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:33:31 2008'' |
