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DOI | 10.1126/science.aav7541 |
Packing of apolar side chains enables accurate design of highly stable membrane proteins | |
Mravic, Marco1; Thomaston, Jessica L.1; Tucker, Maxwell1; Solomon, Paige E.1; Liu, Lijun2,3; DeGrado, William F.1 | |
2019-03-29 | |
发表期刊 | SCIENCE
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ISSN | 0036-8075 |
EISSN | 1095-9203 |
出版年 | 2019 |
卷号 | 363期号:6434页码:1418-+ |
文章类型 | Article |
语种 | 英语 |
国家 | USA; Peoples R China |
英文摘要 | The features that stabilize the structures of membrane proteins remain poorly understood. Polar interactions contribute modestly, and the hydrophobic effect contributes little to the energetics of apolar side-chain packing in membranes. Disruption of steric packing can destabilize the native folds of membrane proteins, but is packing alone sufficient to drive folding in lipids? If so, then membrane proteins stabilized by this feature should be readily designed and structurally characterized-yet this has not been achieved. Through simulation of the natural protein phospholamban and redesign of variants, we define a steric packing code underlying its assembly. Synthetic membrane proteins designed using this code and stabilized entirely by apolar side chains conform to the intended fold. Although highly stable, the steric complementarity required for their folding is surprisingly stringent. Structural informatics shows that the designed packing motif recurs across the proteome, emphasizing a prominent role for precise apolar packing in membrane protein folding, stabilization, and evolution. |
领域 | 地球科学 ; 气候变化 ; 资源环境 |
收录类别 | SCI-E |
WOS记录号 | WOS:000462738000029 |
WOS关键词 | DE-NOVO DESIGN ; TRANSMEMBRANE HELIX ; COMPUTATIONAL DESIGN ; PHOSPHOLAMBAN PENTAMER ; CYSTEINE RESIDUES ; SELF-ASSOCIATION ; POLAR RESIDUES ; ALPHA-HELICES ; COILED-COILS ; STABILITY |
WOS类目 | Multidisciplinary Sciences |
WOS研究方向 | Science & Technology - Other Topics |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://119.78.100.173/C666/handle/2XK7JSWQ/201076 |
专题 | 地球科学 资源环境科学 气候变化 |
作者单位 | 1.Univ Calif San Francisco, Dept Pharmaceut Chem, San Francisco, CA 94158 USA; 2.Peking Univ, Shenzhen Grad Sch, State Key Lab Chem Oncogen, Shenzhen 518055, Peoples R China; 3.DLX Sci, Lawrence, KS 66049 USA |
推荐引用方式 GB/T 7714 | Mravic, Marco,Thomaston, Jessica L.,Tucker, Maxwell,et al. Packing of apolar side chains enables accurate design of highly stable membrane proteins[J]. SCIENCE,2019,363(6434):1418-+. |
APA | Mravic, Marco,Thomaston, Jessica L.,Tucker, Maxwell,Solomon, Paige E.,Liu, Lijun,&DeGrado, William F..(2019).Packing of apolar side chains enables accurate design of highly stable membrane proteins.SCIENCE,363(6434),1418-+. |
MLA | Mravic, Marco,et al."Packing of apolar side chains enables accurate design of highly stable membrane proteins".SCIENCE 363.6434(2019):1418-+. |
条目包含的文件 | 条目无相关文件。 |
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