Greer J
Proc Natl Acad Sci U S A. 1980 Jun;77(6):3393-7. doi: 10.1073/pnas.77.6.3393.
A model has been constructed for haptoglobin heavy chain by using the known sequence homology to the mammalian serine proteases. The three-dimensional structures for three serine proteases, chymotrypsin, trypsin, and elastase, were compared and the structural features that are conserved in all three were extracted. The haptoglobin heavy chain sequence was aligned to the sequences of the three serine proteases by maximizing sequence homology in the regions of conserved structure. The resulting alignment shows that haptoglobin heavy chain must be very closely homologous to these proteases in structure as well as in sequence. Coordinates were derived for the heavy chain by using the homologous structures. The problems associated with these coordinates are outlined and methods for solving them are indicated. The features of the haptoglobin heavy chain structure are described. Implications of the structure for the very strong interaction between this subunit and hemoglobin are discussed.
通过利用与哺乳动物丝氨酸蛋白酶已知的序列同源性,构建了触珠蛋白重链模型。比较了三种丝氨酸蛋白酶(胰凝乳蛋白酶、胰蛋白酶和弹性蛋白酶)的三维结构,并提取了在这三种酶中都保守的结构特征。通过在保守结构区域最大化序列同源性,将触珠蛋白重链序列与这三种丝氨酸蛋白酶的序列进行比对。结果比对表明,触珠蛋白重链在结构和序列上都必须与这些蛋白酶非常紧密地同源。通过使用同源结构得出了重链的坐标。概述了与这些坐标相关的问题,并指出了解决这些问题的方法。描述了触珠蛋白重链结构的特征。讨论了该结构对于该亚基与血红蛋白之间非常强的相互作用的意义。