Xue Feng, Burnett Roger M
The Wistar Institute, 3601 Spruce Street, Philadelphia, PA 19104, USA.
J Struct Biol. 2006 May;154(2):217-21. doi: 10.1016/j.jsb.2005.12.006. Epub 2006 Jan 18.
The major coat protein, hexon, from a chimpanzee adenovirus (AdC68) is of interest as a target for vaccine vector modification. AdC68 hexon has been crystallized in the orthorhombic space group C222 with unit cell dimensions of a = 90.8 A, b = 433.0 A, c = 159.3 A, and one trimer (3 x 104,942 Da) in the asymmetric unit. The crystals diffract to 2.1 A resolution. Initial studies reveal that the molecular arrangement is quite unlike that in hexon crystals for human adenovirus. In the AdC68 crystals, hexon trimers are parallel and pack closely in two-dimensional continuous arrays similar to those formed on electron microscope grids. The AdC68 crystals are the first in which adenovirus hexon has molecular interactions that mimic those used in constructing the viral capsid.
黑猩猩腺病毒(AdC68)的主要衣壳蛋白六邻体,作为疫苗载体修饰的靶点备受关注。AdC68六邻体已在正交空间群C222中结晶,晶胞参数为a = 90.8 Å,b = 433.0 Å,c = 159.3 Å,不对称单元中有一个三聚体(3×104,942 Da)。这些晶体的衍射分辨率达到2.1 Å。初步研究表明,其分子排列与人类腺病毒六邻体晶体中的排列截然不同。在AdC68晶体中,六邻体三聚体相互平行,并紧密堆积成二维连续阵列,类似于在电子显微镜网格上形成的阵列。AdC68晶体是首例腺病毒六邻体具有模拟构建病毒衣壳时所用分子相互作用的晶体。