Sandbox Reserved 935: Difference between revisions

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<Structure load='4OA2' size='350' frame='true' align='right' caption='Insert caption here' scene='57/579705/Testi/1' />
<Structure load='4OA2' size='350' frame='true' align='right' caption='Insert caption here' scene='57/579705/Testi/1' />
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<scene name='57/579705/Nucleotide_binding_pocket/16'>nucleotide binding pocket</scene>


==Introduction==
==Introduction==
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BRI1 belongs to a group of membrane receptor kinases called LRR-RKs with an extracellular LRR ligand binding domain, a single membrane spanning helix and a cytoplasmic kinase domain <ref name=Bojar2014 />. The BRI1 nucleotide binding site is located between the N- and C-lobes of the protein.
BRI1 belongs to a group of membrane receptor kinases called LRR-RKs with an extracellular LRR ligand binding domain, a single membrane spanning helix and a cytoplasmic kinase domain <ref name=Bojar2014 />. The BRI1 nucleotide binding site is located between the N- and C-lobes of the protein.


The kinase domain adopts an active conformation with a salt-bridge between Lysine-911 and Glutamate-927 <ref name=Bojar2014 />. There is also a hydrogen bond between Glutamate-927 and Tyrosine-956. This tyrosine residue is a gatekeeper determining the size of the nucleotide binding pocket. Comparison with other plant receptor-like kinases suggests this hydrogen bond interaction and salt-bridge are important for the activation, because they are holding the binding pocket in its active conformation.
The kinase domain <scene name='57/579705/Nucleotide_binding_pocket/16'>nucleotide binding pocket</scene> adopts an active conformation with a salt-bridge between Lysine-911 and Glutamate-927 <ref name=Bojar2014 />. There is also a hydrogen bond between Glutamate-927 and Tyrosine-956. This tyrosine residue is a gatekeeper determining the size of the nucleotide binding pocket. Comparison with other plant receptor-like kinases suggests this hydrogen bond interaction and salt-bridge are important for the activation, because they are holding the binding pocket in its active conformation.


==Function==
==Function==