Difference between revisions of "Part:BBa K404210"
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===Usage and Biology=== | ===Usage and Biology=== | ||
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| + | The primary receptor of AAV-2 is the heparan sulfate proteoglycan (HSPG) receptor (Perabo et al. 2006). Its binding motif consists of five amino-acids located on the capsid surface: R484/R487, K532, R585/587. (Trepel et al. 2009). | ||
| + | The positively charged arginine residues interact with the HSPGs' negatively charged acid residues. Opie et al. have shown that two point mutations (R585A and R588A) are sufficient to eliminate the heparin binding affinity in AAV2. | ||
| + | (Opie et al. 2003). This ViralBrick has been created to introduce this knockout into other constructs. The biobricks with containing this knockout are annotated with „HSPG-ko“. | ||
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| + | <div style="float:right; width:480px; height:auto; "><img src="https://static.igem.org/mediawiki/2010/0/04/Freiburg10_HSPG_binding_motif.png" width="460" | ||
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| + | ===Restriction sites]] | ||
<table border="1" style="float:right; width:480px; height:auto;> | <table border="1" style="float:right; width:480px; height:auto;> | ||
<tr> | <tr> | ||
Revision as of 18:54, 26 October 2010
ViralBrick-587KO-Empty
Usage and Biology
The primary receptor of AAV-2 is the heparan sulfate proteoglycan (HSPG) receptor (Perabo et al. 2006). Its binding motif consists of five amino-acids located on the capsid surface: R484/R487, K532, R585/587. (Trepel et al. 2009).
The positively charged arginine residues interact with the HSPGs' negatively charged acid residues. Opie et al. have shown that two point mutations (R585A and R588A) are sufficient to eliminate the heparin binding affinity in AAV2.
(Opie et al. 2003). This ViralBrick has been created to introduce this knockout into other constructs. The biobricks with containing this knockout are annotated with „HSPG-ko“.
===Restriction sites]]