Difference between revisions of "Part:BBa K404008"
| (One intermediate revision by the same user not shown) | |||
| Line 22: | Line 22: | ||
|} | |} | ||
<html> | <html> | ||
| − | The viral capsid is formed by the three structural proteins VP1, VP2 and VP3 which are encoded by the cap gene in an overlapping reading frame. They form an icosahedral symmetry arranged in a stoichiometric ratio of 1:1:10. The mRNA encoding for the cap proteins is transcribed from p40 and alternative spliced to minor and major products. | + | The viral capsid is formed by the three structural proteins VP1, VP2 and VP3 which are encoded by the cap gene in an overlapping reading frame. They form an icosahedral symmetry arranged in a stoichiometric ratio of 1:1:10. The mRNA encoding for the cap proteins is transcribed from p40 and alternative spliced to minor and major products. Whereas VP1 is translated from the minor spliced mRNA, VP2 and VP3 are translated from the major spliced mRNA. The minor spliced product is approximately 10-fold less abundant than the major spliced mRNA. Thus, there is much less VP1 than VP2 and VP3 resulting in a capsid stoichiometric ratio of 1:1:10. The N terminus of VP1 has an extension of 65 amino acids including an additional extension of 138 N-terminal amino acids forming the unique portion of VP1. It contains a motiv of about 70 amino acids that is highly homologous to a phospholipase A2 (PLA2) domain. Furthermore, there are nuclear localization sequences (NLS) which are supposed to be necessary for endosomal escape and nuclear entry. |
| − | |||
<h3>References</h3> | <h3>References</h3> | ||
<b>Bleker, Pawlita, & Kleinschmidt</b>, 2006. Impact of capsid conformation and rep-capsid interactions on adeno-associated virus type 2 genome packaging. Journal of Virology, 810–820 <br /> | <b>Bleker, Pawlita, & Kleinschmidt</b>, 2006. Impact of capsid conformation and rep-capsid interactions on adeno-associated virus type 2 genome packaging. Journal of Virology, 810–820 <br /> | ||
Latest revision as of 21:02, 27 October 2010
[AAV2]-VP1
| AAV2-VP1 | |
|---|---|
| BioBrick Nr. | BBa_K404008 |
| RFC standard | RFC 25 |
| Requirement | pSB1C3_001 |
| Source | pAAV_RC from Stratagene |
| Submitted by | [http://2010.igem.org/Team:Freiburg_Bioware FreiGEM 2010] |
The viral capsid is formed by the three structural proteins VP1, VP2 and VP3 which are encoded by the cap gene in an overlapping reading frame. They form an icosahedral symmetry arranged in a stoichiometric ratio of 1:1:10. The mRNA encoding for the cap proteins is transcribed from p40 and alternative spliced to minor and major products. Whereas VP1 is translated from the minor spliced mRNA, VP2 and VP3 are translated from the major spliced mRNA. The minor spliced product is approximately 10-fold less abundant than the major spliced mRNA. Thus, there is much less VP1 than VP2 and VP3 resulting in a capsid stoichiometric ratio of 1:1:10. The N terminus of VP1 has an extension of 65 amino acids including an additional extension of 138 N-terminal amino acids forming the unique portion of VP1. It contains a motiv of about 70 amino acids that is highly homologous to a phospholipase A2 (PLA2) domain. Furthermore, there are nuclear localization sequences (NLS) which are supposed to be necessary for endosomal escape and nuclear entry.
References
Bleker, Pawlita, & Kleinschmidt, 2006. Impact of capsid conformation and rep-capsid interactions on adeno-associated virus type 2 genome packaging. Journal of Virology, 810–820
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal XhoI site found at 28
Illegal XhoI site found at 214 - 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal SapI site found at 1163