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1Crystal structure of a plant leucine rich repeat protein with two island domains显示文摘Leucine rich repeat(LRR)domain,characterized by a repetitive sequence pattern rich in leucine residues,is a universal protein-protein interaction motif present in all life forms.LRR repeats interrupted by sequences of 30 70 residues(termed island domain,ID)have been found in some plant LRR receptor-like kinases(RLKs)and animal Toll-like receptors(TLR7-9).Recent studies provide insight into how a single ID is structurally integrated into an LRR protein.However,structural information on an LRR protein with two IDs is lacking.The receptor-like protein kinase 2(RPK2)is an LRR-RLK and has important roles in controlling plant growth and development by perception and transduction of hormone signal.Here we present the crystal structure of the extracellular LRR domain of RPK2(RPK2-LRR)containing two IDs from Arabidopsis.The structure reveals that both of the IDs are helical and located at the central region of the single RPK2-LRR solenoid.One of them binds to the inner surface of the solenoid,whereas the other one mainly interacts with the lateral side.Unexpectedly,a long loop immediately following the N-terminal capping domain of RPK2-LRR is presented toward and sandwiched between the two IDs,further stabilizing their embedding to the LRR solenoid.A potential ligand binding site formed by the two IDs and the solenoid is located at the C-terminal side of RPK2-LRR.The structural information of RPK2-LRR broadens our understanding toward the large family of LRR proteins and provides insight into RPK2-mediated signaling.SONG Wen HAN ZhiFu SUN YaDong CHAI JiJie 2014Science China(Life Sciences)2014,57,1:2
2植物受体激酶的结构生物学研究进展--国家自然科学基金重点项目阶段性研究成果综述显示文摘在国家自然科学基金重点项目'植物富含亮氨酸重复序列型受体及其信号转导通路的结构生物学研究'的大力资助下,经过本课题组四年多的努力,我们在植物受体激酶的配体识别及活化机制研究上取得了一系列的重要创新成果,提出了植物受体激酶活化的普遍模式——二聚化模式。本项目的研究奠定了我国在植物受体激酶结构生物学的国际领先地位。韩志富 宋文 王继纵 汤娇 孙亚东 佘继 刘婷婷 刘培源 胡泽汗 柴继杰 2016中国科学基金2016,30,6:0
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