6n4v
CryoEM structure of Leviviridae PP7 WT coat protein dimer capsid (PP7PP7-WT)
Structural highlights
FunctionCAPSD_BPPP7 Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 26 nm in diameter, and consisting of 89 capsid proteins dimers (178 capsid proteins) (PubMed:10739912). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome (By similarity).[UniProtKB:P03612][1] Acts as a translational repressor of viral replicase synthesis late in infection. This latter function is the result of capsid protein interaction with an RNA hairpin which contains the replicase ribosome-binding site.[2] Publication Abstract from PubMedAs 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 Qbeta and MS2, the other Leviviridae-derived VLPs in common use. Engineering the PP7 Virus Capsid as a Peptide Display Platform.,Zhao L, Kopylov M, Potter CS, Carragher B, Finn MG ACS Nano. 2019 Mar 26. doi: 10.1021/acsnano.8b09683. PMID:30912918[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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