2UWI

Structure of CrmE, a poxvirus TNF receptor

Summary for 2UWI

• Entry DOI: 10.2210/pdb2uwi/pdb
• Descriptor: CRME PROTEIN (2 entities in total)
• Functional Keywords: receptor, poxvirus tnf receptor, receptor immunomodulator, tnf alpha receptor
• Biological source: VACCINIA VIRUS
• Total number of polymer chains: 2
• Total formula weight: 31744.06

Authors

Graham, S.C.,Bahar, M.W.,Abrescia, N.G.,Smith, G.L.,Stuart, D.I.,Grimes, J.M. (deposition date: 2007-03-22, release date: 2007-07-10, Last modification date: 2024-11-20)

Primary citation

Graham, S.C.,Bahar, M.W.,Abrescia, N.G.,Smith, G.L.,Stuart, D.I.,Grimes, J.M.
Structure of Crme, a Virus-Encoded Tumour Necrosis Factor Receptor.
J.Mol.Biol., 372:660-, 2007

PubMed Abstract: 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.

PubMed: 17681535
DOI: 10.1016/J.JMB.2007.06.082

Experimental method

X-RAY DIFFRACTION (2 Å)