Jörnvall H, Akusjärvi G, Aleström P, von Bahr-Lindström H, Pettersson U, Appella E, Fowler A V, Philipson L
J Biol Chem. 1981 Jun 25;256(12):6181-6.
The primary structure of the adenovirus hexon polypeptide has been determined by amino acid sequence studies of peptides from all regions of the molecule combined with sequence analysis of selected areas of its gene. The sequence presented contains 966 unique amino acid residues. Overlapping peptides recovered from CNBr cleavage and from digestions with proteolytic enzymes were analyzed, as well as DNA segments around sites for restriction endonucleases in the hexon gene. The primary structure is in good agreement with the total composition of the protein, with the compositions of individual CNBr fragments, and with known locations of restriction enzyme cleavage sites in the gene. Distinct regions of internal homology do not occur in the structure. The entire hexon polypeptide is encoded by a contiguous DNA sequence without intervening sequences.
通过对来自该分子所有区域的肽段进行氨基酸序列研究,并结合对其基因选定区域的序列分析,确定了腺病毒六邻体多肽的一级结构。所呈现的序列包含966个独特的氨基酸残基。分析了从CNBr裂解产物和蛋白酶消化产物中回收的重叠肽段,以及六邻体基因中限制性内切酶切割位点周围的DNA片段。一级结构与蛋白质的总体组成、各个CNBr片段的组成以及基因中已知的限制性酶切位点位置高度一致。该结构中不存在内部同源性的明显区域。整个六邻体多肽由一个连续的DNA序列编码,没有间隔序列。