Amino acid sequence of southern bean mosaic virus coat protein and its relation to the three-dimensional structure of the virus.
Amino acid sequence of southern bean mosaic virus coat protein and its relation to the three-dimensional structure of the virus.
复制标题
南方菜豆花叶病毒外壳蛋白氨基酸序列及其与病毒三维结构的关系
DOI：
10.1016/0042-6822(82)90071-x
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发表时间：
1982
期刊：
影响因子：
3.7
通讯作者：
J. Tremaine
中科院分区：
文献类型：
--
作者：
M. Hermodson;C. Abad;S. Abdel;S. Pundak;M. Rossmann;J. Tremaine
测定了南方菜豆花叶病毒外壳蛋白的氨基酸序列。化学技术得到了2.8分之一分辨率的电子密度图的补充，这有助于确定每个肽的绝对位置。通过与部分已知的南方菜豆花叶病毒RNA序列的比较，插入了四个氨基酸和一个七肽靠近蛋白质的氨基末端的位置。该亚基在面向RNA的一侧上与碱性残基紧密相连。亚基-亚基相互作用是疏水和离子的。准三重轴上的钙位点具有三个谷氨酸残基作为配体。在相对于番茄丛矮病毒结构插入到南方菜豆花叶病毒中的序列内，在Cys 168和176之间存在二硫键。该部分是“β-桶”亚基结构和RNA内部之间的螺旋。
The amino acid sequence of the coat protein of southern bean mosaic virus has been determined. Chemical techniques were supplemented by a 2.8-Å-resolution electron-density map which helped in assigning absolute positions for each peptide. Four amino acids and the placement of one heptapeptide near the amino terminus of the protein were interpolated by comparison with the partially known southern bean mosaic virus RNA sequence. The subunit is heavily lined with basic residues on the side facing the RNA. Subunit-subunit interactions are hydrophobic and ionic. The calcium site on the quasi-threefold axis has three glutamic residues as ligands. There is a disulfide bond, between Cys 168 and 176, within a sequence which is inserted in southern bean mosaic virus relative to the tomato bushy stunt virus structure. This portion is a helix nestling between the “β-barrel” subunit structure and the RNA interior.
影响因子：
3.4
作者：
S. Harrison
通讯作者：
S. Harrison
来自大肠杆菌 B/r 的 D-半乳糖结合蛋白的氨基酸序列。
DOI：
--
发表时间：
1981
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Mahoney,WC;Hogg,RW;Hermodson,MA
通讯作者：
Hermodson,MA
DOI：
10.1016/s0021-9673(00)88735-x
发表时间：
1981
期刊：
Journal of chromatography
影响因子：
--
作者：
Pearson,JD;Mahoney,WC;Hermodson,MA;Regnier,FE
通讯作者：
Regnier,FE