6B85

Crystal structure of transmembrane protein TMHC4_R

6B85 の概要

• エントリーDOI: 10.2210/pdb6b85/pdb
• 分子名称: TMHC4_R (1 entity in total)
• 機能のキーワード: de novo design, multipass transmembrane protein, helical bundle, helical repeat protein, membrane protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 100489.12

構造登録者

Lu, P.,DiMaio, F.,Min, D.,Bowie, J.,Wei, K.Y.,Baker, D. (登録日: 2017-10-05, 公開日: 2018-03-14, 最終更新日: 2024-03-13)

主引用文献

Lu, P.,Min, D.,DiMaio, F.,Wei, K.Y.,Vahey, M.D.,Boyken, S.E.,Chen, Z.,Fallas, J.A.,Ueda, G.,Sheffler, W.,Mulligan, V.K.,Xu, W.,Bowie, J.U.,Baker, D.
Accurate computational design of multipass transmembrane proteins.
Science, 359:1042-1046, 2018

PubMed Abstract: 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.

PubMed: 29496880
DOI: 10.1126/science.aaq1739

実験手法

X-RAY DIFFRACTION (3.889 Å)