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- 저자 : Boyken, Scott E. (검색결과 1 건)
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Accurate computational design of multipass transmembrane proteins
Lu, Peilong,Min, Duyoung,DiMaio, Frank,Wei, Kathy Y.,Vahey, Michael D.,Boyken, Scott E.,Chen, Zibo,Fallas, Jorge A.,Ueda, George,Sheffler, William,Mulligan, Vikram Khipple,Xu, Wenqing,Bowie, James U. American Association for the Advancement of Scienc 2018 Science Vol.359 No.6379
<P><B>Membrane protein oligomers by design</B></P><P>In recent years, soluble protein design has achieved successes such as artificial enzymes and large protein cages. Membrane proteins present a considerable design challenge, but here too there have been advances, including the design of a zinc-transporting tetramer. Lu <I>et al.</I> report the design of stable transmembrane monomers, homodimers, trimers, and tetramers with up to eight membrane-spanning regions in an oligomer. The designed proteins adopted the target oligomerization state and localized to the predicted cellular membranes, and crystal structures of the designed dimer and tetramer reflected the design models.</P><P><I>Science</I>, this issue p. 1042</P><P>The computational design of transmembrane proteins with more than one membrane-spanning region remains a major challenge. We report the design of transmembrane monomers, homodimers, trimers, and tetramers with 76 to 215 residue subunits containing two to four membrane-spanning regions and up to 860 total residues that adopt the target oligomerization state in detergent solution. The designed proteins localize to the plasma membrane in bacteria and in mammalian cells, and magnetic tweezer unfolding experiments in the membrane indicate that they are very stable. Crystal structures of the designed dimer and tetramer—a rocket-shaped structure with a wide cytoplasmic base that funnels into eight transmembrane helices—are very close to the design models. Our results pave the way for the design of multispan membrane proteins with new functions.</P>
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