1AHS

CRYSTAL STRUCTURE OF THE TOP DOMAIN OF AFRICAN HORSE SICKNESS VIRUS VP7

1AHS の概要

• エントリーDOI: 10.2210/pdb1ahs/pdb
• 分子名称: AFRICAN HORSE SICKNESS VIRUS (SEROTYPE 4) VP7 (2 entities in total)
• 機能のキーワード: core protein, glycoprotein, coat protein (viral), viral protein
• 由来する生物種: African horsesickness virus
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 40329.39

構造登録者

Stuart, D.,Gouet, P. (登録日: 1996-03-18, 公開日: 1996-11-08, 最終更新日: 2024-05-22)

主引用文献

Basak, A.K.,Gouet, P.,Grimes, J.,Roy, P.,Stuart, D.
Crystal structure of the top domain of African horse sickness virus VP7: comparisons with bluetongue virus VP7.
J.Virol., 70:3797-3806, 1996

PubMed Abstract: The baculovirus-expressed core protein VP7 of African horse sickness virus serotype 4 (AHSV-4) has been purified to homogeneity and crystallized in the presence of 2.8 M urea. The X-ray structure has been solved to a 2.3-Angstroms (1 Angstrom = 0.1 nm) resolution with an Rfactor of 19.8%. The structure of AHSV VP7 reveals that during crystallization, the two-domain protein is cleaved and only the top domain remains. A similar problem was encountered previously with bluetongue virus (BTV) VP7 (whose structure has been reported), showing that the connections between the top and the bottom domains are rather weak for these two distinct orbiviruses. The top domains of both BTV and AHSV VP7 are trimeric and structurally very similar. The electron density maps show that they both possess an extra electron density feature along their molecular threefold axes, which is most likely due to an unidentified ion. The characteristics of the molecular surface of BTV and AHSV VP7 suggest why AHSV VP7 is much less soluble than BTV VP7 and indicate the possibility of attachment to the cell via attachment of an Arg-Gly-Asp (RGD) motif in the top domain of VP7 to a cellular integrin for both of these orbiviruses.

PubMed: 8648715

実験手法

X-RAY DIFFRACTION (2.3 Å)