2UWI

Structure of CrmE, a poxvirus TNF receptor

2UWI の概要

• エントリーDOI: 10.2210/pdb2uwi/pdb
• 分子名称: CRME PROTEIN (2 entities in total)
• 機能のキーワード: receptor, poxvirus tnf receptor, receptor immunomodulator, tnf alpha receptor
• 由来する生物種: VACCINIA VIRUS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31744.06

構造登録者

Graham, S.C.,Bahar, M.W.,Abrescia, N.G.,Smith, G.L.,Stuart, D.I.,Grimes, J.M. (登録日: 2007-03-22, 公開日: 2007-07-10, 最終更新日: 2024-11-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)