Difference between revisions of "Part:BBa K3610001"

 
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The BRI1-associated receptor kinase (BAK1) is a leucin-rich repeat receptor kinase (LRR-RK) which interacts with multiple other LRR-RKs with different functions in hormone signalling and defense response. BAK1 localizes at the plasma membrane and the endosome.
 
The BRI1-associated receptor kinase (BAK1) is a leucin-rich repeat receptor kinase (LRR-RK) which interacts with multiple other LRR-RKs with different functions in hormone signalling and defense response. BAK1 localizes at the plasma membrane and the endosome.
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Among others, BAK1 interacts with the LRR-RKs EF-Tu receptor (EFR),  FLS2 and cold-shock protein receptor (CORE), all of which are pathogen recognition receptors (PRR) in brassicaceae plants. Upon binding of a microbe-associated molecular pattern at the LRR domain of the PRR, BAK1 forms a heterodimer with the PRR which triggers a phosphorylation cascade, leading to upregulation of defense mechanisms.
 
Among others, BAK1 interacts with the LRR-RKs EF-Tu receptor (EFR),  FLS2 and cold-shock protein receptor (CORE), all of which are pathogen recognition receptors (PRR) in brassicaceae plants. Upon binding of a microbe-associated molecular pattern at the LRR domain of the PRR, BAK1 forms a heterodimer with the PRR which triggers a phosphorylation cascade, leading to upregulation of defense mechanisms.
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
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===Functional Parameters===
 
===Functional Parameters===
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Revision as of 15:30, 30 August 2020


BAK1 from Arabidopsis thaliana

The BRI1-associated receptor kinase (BAK1) is a leucin-rich repeat receptor kinase (LRR-RK) which interacts with multiple other LRR-RKs with different functions in hormone signalling and defense response. BAK1 localizes at the plasma membrane and the endosome. The BAK1 protein forms a structure with an extracellular domain with leucin-rich repeats, a single pass transmembrane domain and an intracellular domain with a kinase function.

Among others, BAK1 interacts with the LRR-RKs EF-Tu receptor (EFR), FLS2 and cold-shock protein receptor (CORE), all of which are pathogen recognition receptors (PRR) in brassicaceae plants. Upon binding of a microbe-associated molecular pattern at the LRR domain of the PRR, BAK1 forms a heterodimer with the PRR which triggers a phosphorylation cascade, leading to upregulation of defense mechanisms.


Sequence and Features


Assembly Compatibility:
  • 10
    INCOMPATIBLE WITH RFC[10]
    Illegal SpeI site found at 1560
    Illegal PstI site found at 650
    Illegal PstI site found at 695
    Illegal PstI site found at 985
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal SpeI site found at 1560
    Illegal PstI site found at 650
    Illegal PstI site found at 695
    Illegal PstI site found at 985
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    INCOMPATIBLE WITH RFC[23]
    Illegal SpeI site found at 1560
    Illegal PstI site found at 650
    Illegal PstI site found at 695
    Illegal PstI site found at 985
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal SpeI site found at 1560
    Illegal PstI site found at 650
    Illegal PstI site found at 695
    Illegal PstI site found at 985
  • 1000
    COMPATIBLE WITH RFC[1000]