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Sandbox Reserved 935

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== BRI<sup>1865-1196</sup>ADP (4OA2) ==
== BRI<sup>1865-1196</sup>ADP (4OA2) ==
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[[Image:BRI1.jpg|1500px|Domain structure of BRI1.]]
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[[Image:BRI1.jpg|thumb|center|1200px|alt=Figure|Domain structure of BRI1]]

Revision as of 09:44, 12 May 2014

This Sandbox is Reserved from 01/04/2014, through 30/06/2014 for use in the course "510042. Protein structure, function and folding" taught by Prof Adrian Goldman, Tommi Kajander, Taru Meri, Konstantin Kogan and Juho Kellosalo at the University of Helsinki. This reservation includes Sandbox Reserved 923 through Sandbox Reserved 947.
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Contents

BRI1865-1196ADP (4OA2)

Image:BRI1.jpg
Domain structure of BRI1


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Drag the structure with the mouse to rotate

Introduction

Brassinosteroid insensitive 1 (BRI1) is a membrane receptor that senses brassinosteroides, which are polyhydroxylated steroid hormones. Brassinosteroids control planth growth and development by activating BRI1 and starting a signaling pathway that leads to nuclear thanscription factors being activated. BRI1 is thought to be a dual-specificity kinase and it has structural features reminiscent of both serine/threonine and tyrosine kinases. In the cell, BRI1 cycles between the plasma membrane and endosomes. When not activated, BRI1 is auto-inhibited by its own C-terminal tail as well as auto-phosphorylation of Thr872 and interaction with BRI1 kinase inhibitor protein BKI1 in the kinase domain. BKI1 also contains an N-terminal targeting motif for the plasma membrane. When the extracellular LRR domain gets activated by a brassinosteroid, it causes a reordering of 70 residues and creates a docking platform for the co-recepter SERK (somatic embryogenesis receptor kinase). The C-termini of BRI1 and SERK trans-phosphorylate each other (on Tr211), releasing the BKI1 from BRI1 and allowing BRI1 to phosphorylate immediate downstream signaling components. The BRI1 nucleotide binding site is located between the N- and C-lobes. When an ATP molecule interacts with the nucleotide binding site in the presence of manganese-ions… In this article we will concentrate on the BRI1 kinase domain and its interaction with the nucleotides ATP/ADP.

Structure

Function

Homologs

References

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

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