Steinrauf L K, Chiang M Y, Shiuan D
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana, USA.
J Biochem. 1999 Feb;125(2):422-9. doi: 10.1093/oxfordjournals.jbchem.a022303.
The molecular structure of the amyloid-forming Bence-Jones protein kappa I Bre has been determined by X-ray crystallography at 2.0 A resolution. The fragment from the kappa chain of immunoprotein contains 107 amino acid residues, and polymerizes in the crystal form into a giant helical spiral, surrounding a cylinder of water 50 A in diameter with a repeat of 77.56 A, containing 12 kappa molecules, plus another 12 molecules from neighboring parallel spirals. The resulting structure has many features which have been found or suggested from studies on the protein fibrils found in amyloid deposits. From the results of the X-ray crystal structure a hypothesis is presented for the structure and formation of the amyloid fibril.
通过X射线晶体学在2.0埃分辨率下确定了形成淀粉样蛋白的本斯-琼斯蛋白κI Bre的分子结构。免疫蛋白κ链的片段包含107个氨基酸残基，在晶体中聚合成一个巨大的螺旋状螺旋，围绕着一个直径为50埃的水圆柱体，重复距离为77.56埃，包含12个κ分子，再加上来自相邻平行螺旋的另外12个分子。所得结构具有许多在对淀粉样沉积物中发现的蛋白质原纤维的研究中已发现或提出的特征。根据X射线晶体结构的结果，提出了关于淀粉样原纤维的结构和形成的假说。
