Matthews S, Mikhailov M, Burny A, Roy P
Department of Biochemistry, Imperial College of Science, Technology and Medicine, University of London, UK.
EMBO J. 1996 Jul 1;15(13):3267-74.
In the mature virion, retroviral matrix proteins are found in association with the inner face of the viral membrane. They play a critical role in determining the morphogenesis of virus assembly. We have determined the three-dimensional solution structure of the bovine leukaemia virus (BLV) matrix protein by heteronuclear nuclear magnetic resonance. The protein contains four principal helices that are joined by short, partially structured loops. Despite no sequence similarity with the lentiviruses, the structure shows an intriguing homology with the equivalent protein from the human and simian immunodeficiency viruses. A root-mean-square deviation of 3.78 angstrom is observed over the backbone atoms of 36 equivalent helical positions. The similarity implies a possible common assembly unit for the matrix proteins of type C retroviruses.
在成熟病毒粒子中，逆转录病毒基质蛋白与病毒膜的内表面相关联。它们在决定病毒组装的形态发生过程中起关键作用。我们通过异核核磁共振确定了牛白血病病毒（BLV）基质蛋白的三维溶液结构。该蛋白包含四个主要螺旋，由短的、部分结构化的环连接。尽管与慢病毒没有序列相似性，但该结构与来自人类和猿猴免疫缺陷病毒的等效蛋白显示出有趣的同源性。在36个等效螺旋位置的主链原子上观察到均方根偏差为3.78埃。这种相似性意味着C型逆转录病毒基质蛋白可能存在共同的组装单元。
