6N4V
CryoEM structure of Leviviridae PP7 WT coat protein dimer capsid (PP7PP7-WT)
This is a non-PDB format compatible entry.
Summary for 6N4V
| Entry DOI | 10.2210/pdb6n4v/pdb |
| EMDB information | 0344 |
| Descriptor | Coat protein (1 entity in total) |
| Functional Keywords | t4, icosahedral, pp7, biotechnology, vaccine, drug delivery, virus like particle |
| Biological source | Pseudomonas phage PP7 More |
| Total number of polymer chains | 120 |
| Total formula weight | 3377280.96 |
| Authors | Liangjun, Z.,Kopylov, M.,Potter, C.S.,Carragher, B.,Finn, M.G. (deposition date: 2018-11-20, release date: 2019-04-03, Last modification date: 2024-10-16) |
| Primary citation | Zhao, L.,Kopylov, M.,Potter, C.S.,Carragher, B.,Finn, M.G. Engineering the PP7 Virus Capsid as a Peptide Display Platform. Acs Nano, 13:4443-4454, 2019 Cited by PubMed Abstract: As self-assembling polyvalent nanoscale structures that can tolerate substantial genetic and chemical modification, virus-like particles are useful in a variety of fields. Here we describe the genetic modification and structural characterization of the Leviviridae PP7 capsid protein as a platform for the presentation of functional polypeptides. This particle was shown to tolerate the display of sequences from 1 kDa (a cell penetrating peptide) to 14 kDa (the Fc-binding double Z-domain) on its exterior surface as C-terminal genetic fusions to the coat protein. In addition, a dimeric construct allowed the presentation of exogenous loops between capsid monomers and the simultaneous presentation of two different peptides at different positions on the icosahedral structure. The PP7 particle is thereby significantly more tolerant of these types of polypeptide additions than Qβ and MS2, the other Leviviridae-derived VLPs in common use. PubMed: 30912918DOI: 10.1021/acsnano.8b09683 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
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