Difference between revisions of "Part:BBa K404011"
| Line 1: | Line 1: | ||
| − | |||
__NOTOC__ | __NOTOC__ | ||
<partinfo>BBa_K404011 short</partinfo> | <partinfo>BBa_K404011 short</partinfo> | ||
| + | <html> | ||
| + | The AAV capsid consists of 60 capsid protein subunits. The three cap proteins VP1, VP2, and VP3 are encoded in an overlapping reading frame. Arranged in a stoichiometric ratio of 1:1:10, they form an icosahedral symmetry. The mRNA encoding for the cap proteins is transcribed from p40 and alternative spliced to minor and major products. Alternative splicing and translation initiation of VP2 at a nonconventional ACG initiation codon promote the expression of VP1, VP2 and VP3. The VP proteins share a common C terminus and stop codon, but begin with a different start codon. The translation of VP2 from the major spliced mRNA is not as efficient as of VP1 and VP3 because it initiates at a Thr codon (ACG). The N terminus of VP1 has an extension of 65 amino acids and similar to VP1, it contains two functional elements: a phospholipase A2 (PLA2) domain and nuclear localization signals (BR)(+). These elements are conserved almost in all parvoviruses. The exact role of VP2 remains unknown, although the protein is thought to be nonessential for viral assembly and infectivity. | ||
| + | <center><img src="https://static.igem.org/mediawiki/parts/a/a7/Freiburg10_Cap_proteins_VP1_2%263.png" width="700" | ||
| + | height="auto" margin: 10px 10px 10px 10px/></center> | ||
| − | + | <b> Figure 1: The VP proteins are encoded in an overlapping open reading frame. </b>. | |
| − | < | + | <br/> |
| − | + | <br/> | |
| − | + | <html/> | |
<!-- --> | <!-- --> | ||
<span class='h3bb'>Sequence and Features</span> | <span class='h3bb'>Sequence and Features</span> | ||
Revision as of 23:30, 26 October 2010
pCMV_[AAV2]-VP2 The AAV capsid consists of 60 capsid protein subunits. The three cap proteins VP1, VP2, and VP3 are encoded in an overlapping reading frame. Arranged in a stoichiometric ratio of 1:1:10, they form an icosahedral symmetry. The mRNA encoding for the cap proteins is transcribed from p40 and alternative spliced to minor and major products. Alternative splicing and translation initiation of VP2 at a nonconventional ACG initiation codon promote the expression of VP1, VP2 and VP3. The VP proteins share a common C terminus and stop codon, but begin with a different start codon. The translation of VP2 from the major spliced mRNA is not as efficient as of VP1 and VP3 because it initiates at a Thr codon (ACG). The N terminus of VP1 has an extension of 65 amino acids and similar to VP1, it contains two functional elements: a phospholipase A2 (PLA2) domain and nuclear localization signals (BR)(+). These elements are conserved almost in all parvoviruses. The exact role of VP2 remains unknown, although the protein is thought to be nonessential for viral assembly and infectivity.
