Characterization and crystallization of core streptavidin.
Characterization and crystallization of core streptavidin.
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DOI：
10.1016/s0021-9258(18)47884-2
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发表时间：
1987-10
期刊：
影响因子：
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通讯作者：
A. Pähler;W. Hendrickson;M. A. Kolks;C. Argaraña;C. Cantor
中科院分区：
文献类型：
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作者：
A. Pähler;W. Hendrickson;M. A. Kolks;C. Argaraña;C. Cantor
我们的特点是链霉亲和素产品已减少到最小的大小，仍然保留完整的生物素结合活性。该核心链霉亲和素在与鸡蛋白色亲和素的末端密切对应的点的两端被蛋白水解。核心链霉亲和素比母体分子更可溶。我们已经培养了三种不同类型的核心链霉亲和素晶体。这些晶体的对称性证明了分子是以四面体（D2）点对称组织的四聚体。生物素与核心链霉亲和素相互作用的晶体学反应表明，一些构象变化伴随着配体结合。我们正试图从这些核心链霉亲和素晶体中确定链霉亲和素及其硒生物素复合物的三维结构。
We have characterized a streptavidin product that had been reduced to a minimal size that still retained full biotin-binding activity. This core streptavidin is proteolyzed at both ends at points that correspond closely with the termini of hen egg white avidin. Core streptavidin is more soluble than is the parent molecule. We have grown three different types of crystals of core streptavidin. The symmetry properties of these crystals prove that the molecule is a tetramer organized in tetrahedral (D2) point symmetry. The crystallographic response to the interaction of biotin with core streptavidin indicates that some conformational change accompanies ligand binding. We are attempting to determine the three-dimensional structure of streptavidin and its complex with selenobiotin from these crystals of core streptavidin.