Slingsby C
Trans Ophthalmol Soc U K (1962). 1982;102 Pt 3:337-41.
Although lens structural proteins are extremely diverse, there appear to be common structural motifs or folding units from which the beta-gamma-crystallins can be constructed. X-ray diffraction techniques have solved the atomic three-dimensional structure of monomeric bovine gamma-II. The related protein, beta Bp, the principal subunit of bovine beta-crystallin has been predicted, using computer graphics techniques, to have a similar tertiary structure. These molecular models show the spatial orientation of some of the reactive side-chains which have been implicated in oxidative disruption of lens structure.
尽管晶状体结构蛋白极其多样,但似乎存在一些共同的结构基序或折叠单元,β-γ-晶状体蛋白可由此构建而成。X射线衍射技术已解析出单体牛γ-II的原子三维结构。利用计算机图形技术预测,相关蛋白βBp(牛β-晶状体蛋白的主要亚基)具有相似的三级结构。这些分子模型展示了一些反应性侧链的空间取向,这些侧链与晶状体结构的氧化破坏有关。