Padlan E A, Love W E
J Biol Chem. 1985 Jul 15;260(14):8272-9. doi: 10.2210/pdb1hbs/pdb.
The crystal structure of deoxyhemoglobin S has been refined at 3.0-A resolution using the Hendrickson-Konnert restrained least-squares method. Comparison with the structure of deoxyhemoglobin A reveals a hingelike movement of the beta-chain A helices, which are involved in molecular contacts, toward the EF corners of their respective subunits. This movement brings the amino termini of the beta-chains closer to the molecular dyad. The A helices remain alpha-helical throughout their entire lengths. No other major structural difference is found between deoxyhemoglobin A and deoxyhemoglobin S.
已使用亨德里克森-孔内尔特约束最小二乘法在3.0埃分辨率下对脱氧血红蛋白S的晶体结构进行了精修。与脱氧血红蛋白A的结构比较显示，参与分子接触的β链A螺旋向其各自亚基的EF角发生类似铰链的移动。这种移动使β链的氨基末端更靠近分子二分体。A螺旋在其整个长度上均保持α螺旋结构。在脱氧血红蛋白A和脱氧血红蛋白S之间未发现其他主要结构差异。
