Keefe L J, Sondek J, Shortle D, Lattman E E
Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205-2185.
Proc Natl Acad Sci U S A. 1993 Apr 15;90(8):3275-9. doi: 10.1073/pnas.90.8.3275.
The x-ray crystal structure of a mutant of staphylococcal nuclease that contains a single glycine residue inserted in the C-terminal alpha-helix has been solved to 1.67 A resolution and refined to a crystallographic R value of 0.170. This inserted glycine residue is accommodated in the alpha-helix by formation of a previously uncharacterized bulge, which we term the alpha aneurism. A conformational search of known protein structures has identified the alpha aneurism in a number of protein families, including the histocompatibility antigens and hemoglobins.
已解析出一种葡萄球菌核酸酶突变体的X射线晶体结构，该突变体在C端α螺旋中插入了一个甘氨酸残基，分辨率达到1.67 Å，并精修至晶体学R值为0.170。这个插入的甘氨酸残基通过形成一个以前未被表征的凸起（我们称之为α动脉瘤）容纳在α螺旋中。对已知蛋白质结构的构象搜索在许多蛋白质家族中发现了α动脉瘤，包括组织相容性抗原和血红蛋白。
