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PDBsum entry 3rgz
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References listed in PDB file
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Key reference
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Title
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Structural insight into brassinosteroid perception by bri1.
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Authors
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J.She,
Z.Han,
T.W.Kim,
J.Wang,
W.Cheng,
J.Chang,
S.Shi,
J.Wang,
M.Yang,
Z.Y.Wang,
J.Chai.
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Ref.
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Nature, 2011,
474,
472-476.
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PubMed id
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Abstract
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Brassinosteroids are essential phytohormones that have crucial roles in plant
growth and development. Perception of brassinosteroids requires an active
complex of BRASSINOSTEROID-INSENSITIVE 1 (BRI1) and BRI1-ASSOCIATED KINASE 1
(BAK1). Recognized by the extracellular leucine-rich repeat (LRR) domain of
BRI1, brassinosteroids induce a phosphorylation-mediated cascade to regulate
gene expression. Here we present the crystal structures of BRI1(LRR) in free and
brassinolide-bound forms. BRI1(LRR) exists as a monomer in crystals and solution
independent of brassinolide. It comprises a helical solenoid structure that
accommodates a separate insertion domain at its concave surface. Sandwiched
between them, brassinolide binds to a hydrophobicity-dominating surface groove
on BRI1(LRR). Brassinolide recognition by BRI1(LRR) is through an induced-fit
mechanism involving stabilization of two interdomain loops that creates a
pronounced non-polar surface groove for the hormone binding. Together, our
results define the molecular mechanisms by which BRI1 recognizes
brassinosteroids and provide insight into brassinosteroid-induced BRI1
activation.
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