Difference between revisions of "Part:BBa K3396000"
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===Usage and Biology===
 
===Usage and Biology===
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The DocS[1] module comes from The C. thermocellum scaffoldin and it could recognize and bind tightly to complementary Coh2 modules. The Coh2–DocS pair represents the interaction between two complementary families of protein modules that exhibit divergent specificities and affinities, ranging from one of the highest known affinity constants between two proteins to relatively low-affinity interactions.
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The DocS[1] module comes from The C. thermocellum scaffoldin and it could recognize and bind tightly to complementary Coh2 modules. The Coh2–DocS pair represents a family of constitutively dimerizing protein pairs. They can be used as a proof-of-concept tool to demonstrate whether a split-protein approach works. These pairs can also be replaced with other inducible protein dimerization pairs for signal controlled purposes.
  
  

Revision as of 01:54, 25 October 2020


DocS

The DocS module comes from The C. thermocellum scaffoldin and it could recognize and bind tightly to complementary Coh2 modules.

Usage and Biology

The DocS[1] module comes from The C. thermocellum scaffoldin and it could recognize and bind tightly to complementary Coh2 modules. The Coh2–DocS pair represents a family of constitutively dimerizing protein pairs. They can be used as a proof-of-concept tool to demonstrate whether a split-protein approach works. These pairs can also be replaced with other inducible protein dimerization pairs for signal controlled purposes.


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]


Reference

[1] BARAK Y, HANDELSMAN T, NAKAR D, et al. Matching fusion protein systems for affinity analysis of two interacting families of proteins: the cohesin-dockerin interaction [J]. J Mol Recognit, 2005, 18(6): 491-501.