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The X-ray three-dimensional structure of avidin

机译:抗生物素蛋白的X射线三维结构

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Avidin is a basic, highly stable, homotetrameric protein, isolated from bird egg-white, binding up to four molecules of D-biotin with extremely high affinity (K_d approx l0~(-15) M). The protein has been the object of different crystallographic investigations. In all the crystal structures, the four avidin subunits display almost exact 222 symmetry. Each avidin chain (128 amino acids) is arranged in a eight-stranded antiparallel #beta#-barrel. whose inner region defines the D-biotin binding site. The molecular bases of D-biotin affinity can be recognised in a fairly rigid binding site. which is sterically complementary to the shape and polarity of the incoming vitamin, and is readily accessible in the apoprotein structure. Avidin displays remarkable structural and functional relationships to the acidic protein sretpavidin, isolated from Streptomyces avidinii.
机译:抗生物素蛋白是一种基本的,高度稳定的,同源四聚体蛋白,从鸟蛋清中分离出来,以极高的亲和力(K_d约10〜(-15)M)结合多达四个D-生物素分子。该蛋白质已成为不同晶体学研究的对象。在所有晶体结构中,四个抗生物素蛋白亚基均显示出几乎精确的222对称性。每个抗生物素蛋白链(128个氨基酸)排列在八链反平行#beta#桶中。其内部区域定义了D-生物素结合位点。 D-生物素亲和力的分子碱基可以在相当刚性的结合位点识别。它与输入的维生素的形状和极性在空间上互补,并且易于在脱辅基蛋白结构中获得。抗生物素蛋白与从抗生物素蛋白链霉菌分离的酸性蛋白sretpavidin具有显着的结构和功能关系。

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