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.
Frontiers in bioscience : a journal and virtual library
May 29, 2008
Agency: NIGMS NIH HHS, Id: GM079689
Agency: NIGMS NIH HHS, Id: R01 GM079689
Agency: NIGMS NIH HHS, Id: R01 GM079689-01A1
Agency: NIGMS NIH HHS, Id: R01 GM079689-02
Agency: NIAID NIH HHS, Id: R21 AI078708
Agency: NIAID NIH HHS, Id: R21 AI078708-01A1
Protein Processing, Post-Translational
src Homology Domains
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