1yq8
From Proteopedia
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/P5_BPPRD P5_BPPRD] In association with P31 and P2, forms the spike complexes located at the 5-fold vertices of the capsid. Essential for viral infectivity.<ref>PMID:10956048</ref> | [https://www.uniprot.org/uniprot/P5_BPPRD P5_BPPRD] In association with P31 and P2, forms the spike complexes located at the 5-fold vertices of the capsid. Essential for viral infectivity.<ref>PMID:10956048</ref> | ||
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| - | == Publication Abstract from PubMed == | ||
| - | Comparisons of bacteriophage PRD1 and adenovirus protein structures and virion architectures have been instrumental in unraveling an evolutionary relationship and have led to a proposal of a phylogeny-based virus classification. The structure of the PRD1 spike protein P5 provides further insight into the evolution of viral proteins. The crystallized P5 fragment comprises two structural domains: a globular knob and a fibrous shaft. The head folds into a ten-stranded jelly roll beta barrel, which is structurally related to the tumor necrosis factor (TNF) and the PRD1 coat protein domains. The shaft domain is a structural counterpart to the adenovirus spike shaft. The structural relationships between PRD1, TNF, and adenovirus proteins suggest that the vertex proteins may have originated from an ancestral TNF-like jelly roll coat protein via a combination of gene duplication and deletion. | ||
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| - | The structure of the bacteriophage PRD1 spike sheds light on the evolution of viral capsid architecture.,Merckel MC, Huiskonen JT, Bamford DH, Goldman A, Tuma R Mol Cell. 2005 Apr 15;18(2):161-70. PMID:15837420<ref>PMID:15837420</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
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| - | <div class="pdbe-citations 1yq8" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
PRD1 vertex protein P5
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