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Keeping It Together: Structures, Functions, and Applications of Viral Decoration Proteins |pdf=|usr=}}{{33066635}} gab.com Text Keeping It Together: Structures, Functions, and Applications of Viral Decoration Proteins JO: Viruses http://www.kidney.de/pget.php?&tw=1&pmid=33066635 #FOAvip Decoration proteins are viral accessory gene products that adorn the surfaces of some phages and viral capsids, particularly tailed dsDNA phages. These proteins often play a "cementing" role, reinforcing capsids against accumulating internal pressure due to genome packaging, or environmental insults such as extremes of temperature or pH. Many decoration proteins serve alternative functions, including target cell recognition, participation in viral assembly, capsid size determination, or modulation of host gene expression. Examples that currently have structures characterized to high-resolution fall into five main folding motifs: beta-tulip, beta-tadpole, OB-fold, Ig-like, and a rare knotted alpha-helical fold. Most of these folding motifs have structure homologs in virus and target cell proteins, suggesting horizontal gene transfer was important in their evolution. Oligomerization states of decoration proteins range from monomers to trimers, with the latter most typical. Decoration proteins bind to a variety of loci on capsids that include icosahedral 2-, 3-, and 5-fold symmetry axes, as well as pseudo-symmetry sites. These binding sites often correspond to "weak points" on the capsid lattice. Because of their unique abilities to bind virus surfaces noncovalently, decoration proteins are increasingly exploited for technology, with uses including phage display, viral functionalization, vaccination, and improved nanoparticle design for imaging and drug delivery. These applications will undoubtedly benefit from further advances in our understanding of these versatile augmenters of viral functions. Twit Text FOAVip Keeping It Together: Structures, Functions, and Applications of Viral Decoration Proteins ????Viruses http://www.kidney.de/pget.php?&tw=1&pmid=33066635 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33066635 #FOAvip English Wikipedia <ref>{{Cite pmid|33066635}}</ref> Keeping It Together: Structures, Functions, and Applications of Viral Decoration Proteins #MMPMID33066635 Dedeo CL; Teschke CM; Alexandrescu AT Viruses 2020[Oct]; 12 (10): � PMID33066635show ga Decoration proteins are viral accessory gene products that adorn the surfaces of some phages and viral capsids, particularly tailed dsDNA phages. These proteins often play a "cementing" role, reinforcing capsids against accumulating internal pressure due to genome packaging, or environmental insults such as extremes of temperature or pH. Many decoration proteins serve alternative functions, including target cell recognition, participation in viral assembly, capsid size determination, or modulation of host gene expression. Examples that currently have structures characterized to high-resolution fall into five main folding motifs: beta-tulip, beta-tadpole, OB-fold, Ig-like, and a rare knotted alpha-helical fold. Most of these folding motifs have structure homologs in virus and target cell proteins, suggesting horizontal gene transfer was important in their evolution. Oligomerization states of decoration proteins range from monomers to trimers, with the latter most typical. Decoration proteins bind to a variety of loci on capsids that include icosahedral 2-, 3-, and 5-fold symmetry axes, as well as pseudo-symmetry sites. These binding sites often correspond to "weak points" on the capsid lattice. Because of their unique abilities to bind virus surfaces noncovalently, decoration proteins are increasingly exploited for technology, with uses including phage display, viral functionalization, vaccination, and improved nanoparticle design for imaging and drug delivery. These applications will undoubtedly benefit from further advances in our understanding of these versatile augmenters of viral functions. |Animals[MESH] |Capsid Proteins/chemistry/genetics[MESH] |Capsid/chemistry[MESH] |DNA Packaging[MESH] |DNA Viruses/*genetics[MESH] |DNA, Viral[MESH] |Gene Transfer, Horizontal[MESH] |Host-Pathogen Interactions[MESH] |Mice[MESH] |Models, Molecular[MESH] |Protein Folding[MESH] |Structure-Activity Relationship[MESH] |Viral Proteins/*chemistry/*genetics[MESH] |Virion[MESH]Keeping It Together: Structures, Functions, and Applications of Viral (epmc).pdf DeepDyve Pubget Overpricing