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Structural insight into brassinosteroid perception by BRI1

Title
Structural insight into brassinosteroid perception by BRI1
Author
김태욱
Keywords
Arabidopsis; chemistry; metabolism; Arabidopsis Proteins; Binding Sites; Brassinosteroids; Cholestanols; Crystallography; X-Ray; Enzyme Activation; Hydrophobic and Hydrophilic Interactions; Models; Molecular; Protein Binding; Protein Folding; Protein Kinases; Protein Structure; Tertiary, Steroids; Heterocyclic; Structure-Activity Relationship; Substrate Specificity
Issue Date
2011-06
Publisher
NATURE PUBLISHING GROUP, MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND
Citation
Nature, Vol.474 No.7352 [2011], 472-476
Abstract
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.
URI
http://eds.a.ebscohost.com/eds/detail/detail?vid=0&sid=9ef53694-dbb2-49d5-9ff7-d163bf2a0542%40sessionmgr4008&bdata=Jmxhbmc9a28mc2l0ZT1lZHMtbGl2ZQ%3d%3d#AN=61765860&db=a9hhttp://hdl.handle.net/20.500.11754/37701
ISSN
0028-0836; 1476-4687
DOI
10.1038/nature10178
Appears in Collections:
COLLEGE OF NATURAL SCIENCES[S](자연과학대학) > LIFE SCIENCE(생명과학과) > Articles
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