Seshadri K, Garemyr R, Wallin E, von Heijne G, Elofsson A
Department of Biochemistry, Stockholm University, Sweden.
Protein Sci. 1998 Sep;7(9):2026-32. doi: 10.1002/pro.5560070919.
We have analyzed the known three-dimensional structures of trimeric porins from bacterial outer membranes. The distribution of surface-exposed residues in a direction perpendicular to the membrane is similar to that in helical membrane proteins, with aliphatic residues concentrated in the central 20 A of the bilayer. Outside these residues is a layer of aromatic residues, followed by polar and charged residues. Residues in the trimer interface are more conserved than residues not in the interface. By comparing the interface and noninterface residues, an interface preference scale has been derived that may be used as a basis for predicting interface surfaces in monomer models.
我们分析了来自细菌外膜的三聚体孔蛋白的已知三维结构。在垂直于膜的方向上，表面暴露残基的分布与螺旋膜蛋白中的分布相似，脂肪族残基集中在双层膜中央20埃的区域。在这些残基之外是一层芳香族残基，接着是极性和带电荷的残基。三聚体界面处的残基比非界面处的残基更保守。通过比较界面和非界面残基，得出了一个界面偏好量表，可作为预测单体模型中界面表面的基础。
