Structural analysis of receptor-like kinase SOBIR1 reveals mechanisms that regulate its phosphorylation-dependent activation.

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作者： Xue,Wei ^[1] ; Yulu,Wang ^[1] ; Su,Zhang ^[2] ; Tianyi,Gu ^[1] ; Gabryel,Steinmetz ^[3] ; Haiyan,Yu ^[4] ; Guoguang,Guo ^[1] ; Xin,Liu ^[5] ; Shilong,Fan ^[6] ; Fengzhong,Wang ^[7] ; Yangnan,Gu ^[1] ; Fengjiao,Xin ^[3]

作者单位： Laboratory of Biomanufacturing and Food Engineering, Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100193, China. ^[1] Beijing Advanced Innovation Center for Tree Breeding by Molecular Design, Beijing Forestry University, Beijing 100083, China. ^[2] Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720, USA. ^[3] Innovative Genomics Institute, University of California, Berkeley, CA 94720, USA. ^[4] Key Laboratory of Ministry of Education for Protein Science, School of Life Sciences, Tsinghua University, Beijing 100084, China. ^[5] Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China. ^[6] The Center of Protein Science, Tsinghua University, Beijing 100084, China. ^[7]

关键词 LRR-RLK SOBIR1 autophosphorylation crystal structure stepwise activation unusual architecture

主题词拟南芥属(Arabidopsis);拟南芥蛋白质类(Arabidopsis Proteins);磷酰化(Phosphorylation);蛋白激酶类(Protein Kinases)

DOI 10.1016/j.xplc.2022.100301

PMID 35529948

发布时间 2023-09-16

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Plant communications

2022年3卷2期

100301页

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Structural analysis of receptor-like kinase SOBIR1 reveals mechanisms that regulate its phosphorylation-dependent activation.

Plant communications

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Structural analysis of receptor-like kinase SOBIR1 reveals mechanisms that regulate its phosphorylation-dependent activation.

Plant communications

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Plant communications

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