3K7B

The structure of the poxvirus A33 protein reveals a dimer of unique C-type lectin-like domains.

3K7B の概要

• エントリーDOI: 10.2210/pdb3k7b/pdb
• 分子名称: Protein A33 (2 entities in total)
• 機能のキーワード: c-type lectin-like domain, homodimer, poxvirus, eev, ev, viral protein
• 由来する生物種: Vaccinia virus WR (VACV)
• 細胞内の位置: Virion membrane ; Single-pass type II membrane protein : P68617
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22117.06

構造登録者

Su, H.P.,Garboczi, D.N. (登録日: 2009-10-12, 公開日: 2010-01-19, 最終更新日: 2024-11-20)

主引用文献

Su, H.P.,Singh, K.,Gittis, A.G.,Garboczi, D.N.
The structure of the poxvirus A33 protein reveals a dimer of unique C-type lectin-like domains.
J.Virol., 84:2502-2510, 2010

PubMed Abstract: The current vaccine against smallpox is an infectious form of vaccinia virus that has significant side effects. Alternative vaccine approaches using recombinant viral proteins are being developed. A target of subunit vaccine strategies is the poxvirus protein A33, a conserved protein in the Chordopoxvirinae subfamily of Poxviridae that is expressed on the outer viral envelope. Here we have determined the structure of the A33 ectodomain of vaccinia virus. The structure revealed C-type lectin-like domains (CTLDs) that occur as dimers in A33 crystals with five different crystal lattices. Comparison of the A33 dimer models shows that the A33 monomers have a degree of flexibility in position within the dimer. Structural comparisons show that the A33 monomer is a close match to the Link module class of CTLDs but that the A33 dimer is most similar to the natural killer (NK)-cell receptor class of CTLDs. Structural data on Link modules and NK-cell receptor-ligand complexes suggest a surface of A33 that could interact with viral or host ligands. The dimer interface is well conserved in all known A33 sequences, indicating an important role for the A33 dimer. The structure indicates how previously described A33 mutations disrupt protein folding and locates the positions of N-linked glycosylations and the epitope of a protective antibody.

PubMed: 20032175
DOI: 10.1128/JVI.02247-09

実験手法

X-RAY DIFFRACTION (2.1 Å)