Difference between revisions of "Part:BBa K404006"
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<partinfo>BBa_K404006 short</partinfo> | <partinfo>BBa_K404006 short</partinfo> | ||
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+ | {| style="color:black; margin: 0px 0px 500px 20px;" cellpadding="6" cellspacing="1" border="2" align="right" | ||
+ | ! colspan="2" style="background:#66bbff;"|[https://parts.igem.org/Part:BBa_K404006 AAV2-VP123] | ||
+ | |- | ||
+ | |'''BioBrick Nr.''' | ||
+ | |[https://parts.igem.org/Part:BBa_K404006 BBa_K404006] | ||
+ | |- | ||
+ | |'''RFC standard''' | ||
+ | |[https://parts.igem.org/Help:Assembly_standard_25 RFC 25] | ||
+ | |- | ||
+ | |'''Requirement''' | ||
+ | |pSB1C3<br> | ||
+ | |- | ||
+ | |'''Source''' | ||
+ | |pAAV_RC from Stratagene | ||
+ | |- | ||
+ | |'''Submitted by''' | ||
+ | |[http://2010.igem.org/Team:Freiburg_Bioware FreiGEM 2010] | ||
+ | |} | ||
<html> | <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 N termini of VP1 and VP2 play important roles in infection. The VP1 N-terminus contains motifs that are highly homologous to the phospholipase A2 (PLA2) domain and nuclear localization signals (BR)(+). VP2 contains basic regions, too. | |
− | + | ||
− | + | <h3>References</h3> | |
− | + | <b>DiPrimio, Asokan, Govindasamy, Agbandje-McKenna, & Samulski</b>, June 2008. Surface loop dynamics in adeno-associated virus capsid assembly. Journal of virology, 167(1), 5178–5189 <br /> | |
− | + | <center><img src="https://static.igem.org/mediawiki/parts/a/a7/Freiburg10_Cap_proteins_VP1_2%263.png" width="600" | |
− | 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 N termini of VP1 and VP2 play important roles in infection | + | height="auto"/></center> |
− | + | <b> Figure 1: The VP proteins are encoded in an overlapping open reading frame. </b> | |
− | + | ||
− | <center><img src="https://static.igem.org/mediawiki/parts/a/a7/Freiburg10_Cap_proteins_VP1_2%263.png" width=" | + | |
− | height="auto" | + | |
− | + | ||
− | <b> Figure 1: The VP proteins are encoded in an overlapping open reading frame. </b> | + | |
− | + | ||
− | + | ||
− | + | ||
− | + | ||
</html> | </html> | ||
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Latest revision as of 16:20, 30 October 2010
[AAV2]-VP123
AAV2-VP123 | |
---|---|
BioBrick Nr. | BBa_K404006 |
RFC standard | RFC 25 |
Requirement | pSB1C3 |
Source | pAAV_RC from Stratagene |
Submitted by | [http://2010.igem.org/Team:Freiburg_Bioware FreiGEM 2010] |
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 N termini of VP1 and VP2 play important roles in infection. The VP1 N-terminus contains motifs that are highly homologous to the phospholipase A2 (PLA2) domain and nuclear localization signals (BR)(+). VP2 contains basic regions, too.
References
DiPrimio, Asokan, Govindasamy, Agbandje-McKenna, & Samulski, June 2008. Surface loop dynamics in adeno-associated virus capsid assembly. Journal of virology, 167(1), 5178–5189Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BamHI site found at 1729
Illegal XhoI site found at 31
Illegal XhoI site found at 217 - 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal SapI site found at 1166