7Q1T
A de novo designed hetero-dimeric antiparallel coiled coil apCC-Di-AB
Summary for 7Q1T
Entry DOI | 10.2210/pdb7q1t/pdb |
Descriptor | apCC-Di-A, apCC-Di-B, N-PROPANOL, ... (5 entities in total) |
Functional Keywords | antiparallel, hetero-dimeric, coiled-coil, de novo, protein design, associating peptides, de novo protein |
Biological source | synthetic construct More |
Total number of polymer chains | 2 |
Total formula weight | 6963.95 |
Authors | Shanmugaratnam, S.,Rhys, G.G.,Dawson, W.M.,Woolfson, D.N.,Hocker, B. (deposition date: 2021-10-20, release date: 2022-07-20, Last modification date: 2024-05-01) |
Primary citation | Rhys, G.G.,Cross, J.A.,Dawson, W.M.,Thompson, H.F.,Shanmugaratnam, S.,Savery, N.J.,Dodding, M.P.,Hocker, B.,Woolfson, D.N. De novo designed peptides for cellular delivery and subcellular localisation. Nat.Chem.Biol., 18:999-1004, 2022 Cited by PubMed Abstract: Increasingly, it is possible to design peptide and protein assemblies de novo from first principles or computationally. This approach provides new routes to functional synthetic polypeptides, including designs to target and bind proteins of interest. Much of this work has been developed in vitro. Therefore, a challenge is to deliver de novo polypeptides efficiently to sites of action within cells. Here we describe the design, characterisation, intracellular delivery, and subcellular localisation of a de novo synthetic peptide system. This system comprises a dual-function basic peptide, programmed both for cell penetration and target binding, and a complementary acidic peptide that can be fused to proteins of interest and introduced into cells using synthetic DNA. The designs are characterised in vitro using biophysical methods and X-ray crystallography. The utility of the system for delivery into mammalian cells and subcellular targeting is demonstrated by marking organelles and actively engaging functional protein complexes. PubMed: 35836017DOI: 10.1038/s41589-022-01076-6 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.68 Å) |
Structure validation
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