Sandbox Reserved 935: Difference between revisions

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==Structure==

The BRI1 nucleotide binding site is located between the N- and C-lobes of the protein <ref>Daniel Bojar, Jacobo Martinez, Julia Santiago, Vladimir Rybin, Richard Bayliss and Michael Hothorn: Crystal structures of the phosphorylated BRI1 kinase domain and implications for brassinosteroid signal initiation. The Plant Journal (2014) 78, 31–43. PMID: 24461462 doi: 10.1111/tpj.12445</ref>.

The BRI1 nucleotide binding site is located between the N- and C-lobes of the protein <ref name=Bojar>Daniel Bojar, Jacobo Martinez, Julia Santiago, Vladimir Rybin, Richard Bayliss and Michael Hothorn: Crystal structures of the phosphorylated BRI1 kinase domain and implications for brassinosteroid signal initiation. The Plant Journal (2014) 78, 31–43. PMID: 24461462 doi: 10.1111/tpj.12445</ref>.

The kinase domain adopts an active conformation with a salt-bridge between Lys911 and Glu927 <ref>Daniel Bojar, Jacobo Martinez, Julia Santiago, Vladimir Rybin, Richard Bayliss and Michael Hothorn: Crystal structures of the phosphorylated BRI1 kinase domain and implications for brassinosteroid signal initiation. The Plant Journal (2014) 78, 31–43. PMID: 24461462 doi: 10.1111/tpj.12445</ref>. There is also a hydrogen bond between Glu927 and Tyr956. 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.

The kinase domain adopts an active conformation with a salt-bridge between Lys911 and Glu927 <ref name=Bojar>Daniel Bojar, Jacobo Martinez, Julia Santiago, Vladimir Rybin, Richard Bayliss and Michael Hothorn: Crystal structures of the phosphorylated BRI1 kinase domain and implications for brassinosteroid signal initiation. The Plant Journal (2014) 78, 31–43. PMID: 24461462 doi: 10.1111/tpj.12445</ref>. There is also a hydrogen bond between Glu927 and Tyr956. 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.

==Function==

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@@ Line 24: / Line 24: @@
 ==Structure==
-The BRI1 nucleotide binding site is located between the N- and C-lobes of the protein <ref>Daniel Bojar, Jacobo Martinez, Julia Santiago, Vladimir Rybin, Richard Bayliss and Michael Hothorn: Crystal structures of the phosphorylated BRI1 kinase domain and implications for brassinosteroid signal initiation. The Plant Journal (2014) 78, 31–43. PMID: 24461462 doi: 10.1111/tpj.12445</ref>.
+The BRI1 nucleotide binding site is located between the N- and C-lobes of the protein <ref name=Bojar>Daniel Bojar, Jacobo Martinez, Julia Santiago, Vladimir Rybin, Richard Bayliss and Michael Hothorn: Crystal structures of the phosphorylated BRI1 kinase domain and implications for brassinosteroid signal initiation. The Plant Journal (2014) 78, 31–43. PMID: 24461462 doi: 10.1111/tpj.12445</ref>.
-The kinase domain adopts an active conformation with a salt-bridge between Lys911 and Glu927 <ref>Daniel Bojar, Jacobo Martinez, Julia Santiago, Vladimir Rybin, Richard Bayliss and Michael Hothorn: Crystal structures of the phosphorylated BRI1 kinase domain and implications for brassinosteroid signal initiation. The Plant Journal (2014) 78, 31–43. PMID: 24461462 doi: 10.1111/tpj.12445</ref>. There is also a hydrogen bond between Glu927 and Tyr956. 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.
+The kinase domain adopts an active conformation with a salt-bridge between Lys911 and Glu927 <ref name=Bojar>Daniel Bojar, Jacobo Martinez, Julia Santiago, Vladimir Rybin, Richard Bayliss and Michael Hothorn: Crystal structures of the phosphorylated BRI1 kinase domain and implications for brassinosteroid signal initiation. The Plant Journal (2014) 78, 31–43. PMID: 24461462 doi: 10.1111/tpj.12445</ref>. There is also a hydrogen bond between Glu927 and Tyr956. 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.
 ==Function==