Difference between revisions of "Part:BBa K4389007"
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<partinfo>BBa_K4389007 short</partinfo> | <partinfo>BBa_K4389007 short</partinfo> | ||
| − | A24 protein from Vaccinia virus | + | A24 protein from the Vaccinia virus |
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| + | ===Usage and Biology=== | ||
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| + | A27 is a 110 amino acids protein, that consist of the heparin-binding domain, a coiled-coil domain, and the A17 binding leucine zipper domain. The heparin-binding domain contains 21-34 amino acids and has the core sequence KKPE, which is 26-29 amino acids. KKPE is essential for heparin sulfate attachment. Coiled-coil domain, 43-84 amino acids, contributes to self-oligomerization in vitro. Two cysteines at 71 and 72 create a disulfide bond for the self-assembly of A27 and interact with A26. The crystal structure of A27 is a trimeric assembly, consisting of three α-helices, two parallel and one antiparallel. Trimerization can be observed in the N-terminal section. Interaction between trimers occurs at the C-terminal region | ||
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| + | ===Reference=== | ||
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| + | Chang, T. H., Chang, S. J., Hsieh, F. L., Ko, T. P., Lin, C. T., Ho, M. R., ... & Wang, A. H. (2013). Crystal structure of vaccinia viral A27 protein reveals a novel structure critical for its function and complex formation with A26 protein. PLoS pathogens, 9(8), e1003563. | ||
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Latest revision as of 14:09, 9 October 2022
A27 protein encoding sequence
A24 protein from the Vaccinia virus
Usage and Biology
A27 is a 110 amino acids protein, that consist of the heparin-binding domain, a coiled-coil domain, and the A17 binding leucine zipper domain. The heparin-binding domain contains 21-34 amino acids and has the core sequence KKPE, which is 26-29 amino acids. KKPE is essential for heparin sulfate attachment. Coiled-coil domain, 43-84 amino acids, contributes to self-oligomerization in vitro. Two cysteines at 71 and 72 create a disulfide bond for the self-assembly of A27 and interact with A26. The crystal structure of A27 is a trimeric assembly, consisting of three α-helices, two parallel and one antiparallel. Trimerization can be observed in the N-terminal section. Interaction between trimers occurs at the C-terminal region
Reference
Chang, T. H., Chang, S. J., Hsieh, F. L., Ko, T. P., Lin, C. T., Ho, M. R., ... & Wang, A. H. (2013). Crystal structure of vaccinia viral A27 protein reveals a novel structure critical for its function and complex formation with A26 protein. PLoS pathogens, 9(8), e1003563.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]