Lawrence M C, Suzuki E, Varghese J N, Davis P C, Van Donkelaar A, Tulloch P A, Colman P M
CSIRO Division of Biotechnology, Parkville, Victoria, Australia.
EMBO J. 1990 Jan;9(1):9-15. doi: 10.1002/j.1460-2075.1990.tb08074.x.
The polypeptides of the trimeric seed storage protein phaseolin comprise two structurally similar units each made up of a beta-barrel and an alpha-helical domain. The beta-barrel has the 'jelly-roll' folding topology of the viral coat proteins and the alpha-helical domain shows structural similarity to the helix-turn-helix motif found in certain DNA-binding proteins.
三聚体种子贮藏蛋白菜豆蛋白的多肽包含两个结构相似的单元,每个单元由一个β-桶和一个α-螺旋结构域组成。β-桶具有病毒外壳蛋白的“果冻卷”折叠拓扑结构,α-螺旋结构域与某些DNA结合蛋白中发现的螺旋-转角-螺旋基序具有结构相似性。