Sandbox Reserved 935: Difference between revisions

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BRI1 is a dual-specificity kinase: it can both autophosphorylate on tyrosine residues in the kinase and juxtamembrabe domains (residues 814-865, part of which is not in this model) and also transphosphorylate tyrosine residues in other proteins. The juxtamembrane domain is important for the kinase domain activity.

In this structure, the adenine and ribose parts of ADP are well ordered, whereas the diphosphate is more flexible. BRI<sup>865-1196</sup> can't efficiently hydrolyse ATP to ADP and to a lesser extent GTP to GDP.

In this structure, the adenine and ribose parts of ADP are well ordered, whereas the diphosphate is more flexible. There are hydrogen-bonding interactions of the adenine base and ribose with the BRI1 hinge region main chain atoms (E957, M959) and with two water molecules. When it was an ATP, the catalytic D1009 caused it to γ -phosphate to face outwards. BRI<sup>865-1196</sup> can efficiently hydrolyse ATP to ADP and to a lesser extent GTP to GDP.

==Homologs==

Orthologs for BRI1 can be found from other plant species and they have a similar domain structure in the whole protein. Kinase domain of BRI1 is not specific only for plants as homologs for the kinase domain can be found also from the animals. Closest homolog in human and mouse is called interleukin-1 receptor-associated kinase 4 (IRAK4).

==References==

Sandbox Reserved 935: Difference between revisions

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@@ Line 31: / Line 31: @@
 BRI1 is a dual-specificity kinase: it can both autophosphorylate on tyrosine residues in the kinase and juxtamembrabe domains (residues 814-865, part of which is not in this model) and also transphosphorylate tyrosine residues in other proteins. The juxtamembrane domain is important for the kinase domain activity.
-In this structure, the adenine and ribose parts of ADP are well ordered, whereas the diphosphate is more flexible. BRI<sup>865-1196</sup> can't efficiently hydrolyse ATP to ADP and to a lesser extent GTP to GDP.
+In this structure, the adenine and ribose parts of ADP are well ordered, whereas the diphosphate is more flexible. There are hydrogen-bonding interactions of the adenine base and ribose with the BRI1 hinge region main chain atoms (E957, M959) and with two water molecules. When it was an ATP, the catalytic D1009 caused it to γ -phosphate to face outwards. BRI<sup>865-1196</sup> can efficiently hydrolyse ATP to ADP and to a lesser extent GTP to GDP.
 ==Homologs==
-Orthologs for BRI1 can be found from other plant species and they have a similar domain structure in the whole protein. Kinase domain of BRI1 is not specific only for plants as homologs for the kinase domain can be found also from the animals. Closest homolog in human and mouse is called interleukin-1 receptor-associated kinase 4 (IRAK4).
 ==References==