Difference between revisions of "Part:BBa K4389005"

 
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L1 protein from Vaccinia firus
 
L1 protein from Vaccinia firus
  
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===Usage and Biology===
 
===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 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
  
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>

Revision as of 14:05, 9 October 2022


L1 protein encoding sequence

L1 protein from Vaccinia firus

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

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]