Whitley P, Nilsson I, von Heijne G
Department of Biochemistry, Stockholm University, Sweden.
Nat Struct Biol. 1994 Dec;1(12):858-62. doi: 10.1038/nsb1294-858.
We have designed integral membrane proteins with one, two and four hydrophobic transmembrane segments of highly simplified amino acid composition and with appropriately placed positively charged lysine residues intended to control the overall membrane orientation. When expressed in Escherichia coli, these model proteins insert efficiently into the inner membrane and adopt the predicted topologies. This demonstrates the feasibility of de novo design of multi-spanning integral membrane proteins, and opens up new possibilities for membrane protein engineering.
我们设计了具有高度简化氨基酸组成的一个、两个和四个疏水跨膜片段的整合膜蛋白,并带有适当位置的带正电荷的赖氨酸残基,旨在控制整体膜取向。当在大肠杆菌中表达时,这些模型蛋白能有效地插入内膜并采用预测的拓扑结构。这证明了从头设计多跨膜整合膜蛋白的可行性,并为膜蛋白工程开辟了新的可能性。