Pearl L H, Taylor W R
Nature. 1987;329(6137):351-4. doi: 10.1038/329351a0.
In many retroviruses the 5' end of the pol gene codes for a protease vital for the processing of the gag polyprotein into the separate core proteins. In some viruses this protease is encoded at the 3' end of the gag gene, or between the gag and pol genes in a different reading frame to either. A sequence, Asp-Thr-Gly, which is conserved in retroviral proteases is also conserved in the active sites of aspartic proteases, an observation which has led to the suggestion that the retroviral proteases could belong to this family. We have examined the sequences of the aspartic and retroviral protease families, using pattern-recognition, structure prediction and molecular modelling techniques, and conclude that the viral protease sequences probably correspond to a single domain of an aspartic protease and may function in a dimeric form. We have constructed a model of the pol-protease of human immunodeficiency virus 1 (HIV-1) to test this hypothesis.
在许多逆转录病毒中，pol基因的5'端编码一种蛋白酶，该蛋白酶对于将gag多聚蛋白加工成单独的核心蛋白至关重要。在一些病毒中，这种蛋白酶编码于gag基因的3'端，或者位于gag和pol基因之间，但阅读框与二者均不同。在逆转录病毒蛋白酶中保守的天冬氨酸-苏氨酸-甘氨酸序列，在天冬氨酸蛋白酶的活性位点也保守，这一观察结果提示逆转录病毒蛋白酶可能属于这个家族。我们利用模式识别、结构预测和分子建模技术，研究了天冬氨酸蛋白酶家族和逆转录病毒蛋白酶家族的序列，得出结论：病毒蛋白酶序列可能对应于天冬氨酸蛋白酶的一个结构域，并且可能以二聚体形式发挥作用。我们构建了人类免疫缺陷病毒1（HIV-1）的pol蛋白酶模型来验证这一假说。
