4j0m | pdb_00004j0m
Crystal structure of BRL1 (LRR) in complex with brassinolide
Structural highlights
FunctionBRL1_ARATH Receptor with a serine/threonine-protein kinase activity. Regulates, in response to brassinosteroid binding, a signaling cascade involved in plant development. Binds brassinolide. May be involved in cell growth and vascular differentiation.[1] [2] Publication Abstract from PubMedBrassinosteroids, a group of plant steroid hormones, regulate many aspects of plant growth and development. We and other have previously solved the crystal structures of BRI1(LRR) in complex with brassinolide, the most active brassinosteroid identified thus far. Although these studies provide a structural basis for the recognition of brassinolide by its receptor BRI1, it still remains poorly understood how the hormone differentiates among its conserved receptors. Here we present the crystal structure of the BRI1 homolog BRL1 in complex with brassinolide. The structure shows that subtle differences around the brassinolide binding site can generate a striking effect on its recognition by the BRI1 family of receptors. Structural comparison of BRL1 and BRI1 in their brassinolide-bound forms reveals the molecular basis for differential binding of brassinolide to its different receptors, which can be used for more efficient design of plant growth regulators for agricultural practice. On the basis of our structural studies and others' data, we also suggest possible mechanisms for the activation of BRI1 family receptors. Structural basis for differential recognition of brassinolide by its receptors.,She J, Han Z, Zhou B, Chai J Protein Cell. 2013 Jun;4(6):475-82. doi: 10.1007/s13238-013-3027-8. Epub 2013 May, 25. PMID:23709366[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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