Difference between revisions of "Part:BBa K4389005"

Latest revision as of 14:06, 9 October 2022

L1 protein encoding sequence

L1 protein from Vaccinia firus

Usage and Biology

L1 is 250 aa myristoylated transmembrane protein that has six cysteines. It can be found on intracellular mature virion of the virus. L1 has a dimer 3D structure with three disulfide bonds

Reference

Su, H. P., Garman, S. C., Allison, T. J., Fogg, C., Moss, B., & Garboczi, D. N. (2005). The 1.51-Å structure of the poxvirus L1 protein, a target of potent neutralizing antibodies. Proceedings of the National Academy of Sciences, 102(12), 4240-4245.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

@@ Line 6: / Line 6: @@
 ===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 it interacts 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
+L1 is 250 aa myristoylated transmembrane protein that has six cysteines. It can be found on intracellular mature virion of the virus. L1 has a dimer 3D structure with three disulfide bonds
+===Reference===
+Su, H. P., Garman, S. C., Allison, T. J., Fogg, C., Moss, B., & Garboczi, D. N. (2005). The 1.51-Å structure of the poxvirus L1 protein, a target of potent neutralizing antibodies. Proceedings of the National Academy of Sciences, 102(12), 4240-4245.
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