Journal
FRONTIERS IN BIOSCIENCE
Volume 13, Issue -, Pages 6455-6471Publisher
FRONTIERS IN BIOSCIENCE INC
DOI: 10.2741/3166
Keywords
motif; disease; virus; drugs; posttranslational modification; review
Categories
Funding
- NIAID NIH HHS [R21 AI078708, R21 AI078708-01A1] Funding Source: Medline
- NIGMS NIH HHS [R01 GM079689, GM079689, R01 GM079689-01A1, R01 GM079689-02] Funding Source: Medline
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Short functional peptide motifs cooperate in many molecular functions including protein interactions, protein trafficking, and posttranslational modifications. Viruses exploit these motifs as a principal mechanism for hijacking cells and many motifs are necessary for the viral life-cycle. A virus can accommodate many short motifs in its small genome size providing a plethora of ways for the virus to acquire host molecular machinery. Host enzymes that act on motifs such as kinases, proteases, and lipidation enzymes, as well as protein interaction domains, are commonly mutated in human disease, suggesting that the short peptide motif targets of these enzymes may also be mutated in disease; however, this is not observed. How can we explain why viruses have evolved to be so dependent on motifs, yet these motifs, in general do not seem to be as necessary for human viability? We propose that short motifs are used at the system level. This system architecture allows viruses to exploit a motif, whereas the viability of the host is not affected by mutation of a single motif.
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