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| 1 | Structure reveals that BAK1 as a co-receptor recognizes the BRIl-bound brassinolide显示文摘 | Yadong Sun Zhlfu Han Jiao Tang Zehan Hu Chengliang Chai Bin Zhou Jijie Chai | 2013 | Cell Research2013，23，11： | 24 |
| 2 | Signature motif-guided identification of receptors for peptide hormones essential for root meristem growth显示文摘发信号的调停肽的 cell-to-cell 在植物在细胞的功能的协作和定义有关键角色。肽受体匹配为理解位于调停肽的发信号下面的机制是重要的。这里,我们报导根分裂组织生长的指导结构的鉴定为植物开发重要的因素(RGF ) 受体。基于签名 ligand 识别,主题(Arg-x-Arg ) 在充满白氨酸的重复受体 kinases (LRR-RKs ) 的一个亚科保存了的试金识别了机能上地 uncharacterized LRR-RK At4g26540 作为 RGF1 (RGFR1 ) 的受体。我们进一步在 2.6 Å 的一个决定与 RGFR1 的 LRR 领域在建筑群解决了 RGF1 的水晶结构;,它表明 Arg-x-Gly-Gly (RxGG ) 主题为由 RGFR1 的 RGF1 的硫酸盐组的特定的识别负责。基于 RxGG 主题,我们识别了另外四 RGFR。在导致 RGF 的发信号的五 RGFR 的参予被生物化学、基因的数据支持。我们也提供证明 SERK 为 RGF 作为合作受体工作的证据。一起拿,我们的学习识别 RGF 受体,能连接 RGF 的合作受体与他们的下游的部件发信号并且为与他们的肽 ligands 的 LRR-RKs 的基于结构的匹配提供原则的一个证明。 | Wen Song Li Liu Jizong Wang Zhen Wu Heqiao Zhang Jiao Tang Guangzhong Lin Yichuan Wang Xing Wen Wenyang Li Zhifu Han Hongwei Guo Jijie Chai | 2016 | Cell Research2016，26，6： | 20 |
| 3 | Structural basis for recognition of an endogenous peptide by the plant receptor kinase PEPR1显示文摘在从他们的先锋蛋白质 PROPEP1-8 的保存 C 终端部分成熟的 Arabidopsis 的内长的肽 AtPep1-8 分别地。二相应充满白氨酸的重复受体 kinases (LRR-RKs ) PEPR1 和 PEPR2 充当 AtPeps 的受体。AtPep 绑定与分享的受体 LRR-RK BAK1 导致 PEPR1,2 的稳定的协会,得到类似于病原体导致的那些的有免疫力的回答。这里,我们与 AtPep1 在建筑群报导 PEPR1 (PEPR1LRR ) 的细胞外的 LRR 领域的水晶结构。结构表明 AtPep1 采用充分扩大的符合构造并且绑在 superhelical PEPR1LRR 的内部表面。生物化学的试金证明 AtPep1 能够导致 PEPR1LRR-BAK1LRR heterodimerization。AtPep1 的保存 C 终端部分统治对 PEPR1LRR 有约束力的 AtPep1,与形成和 PEPR1LRR 的广泛的相互作用的 AtPep1 Asn23 的最后氨基酸。AtPep1 的最后残余的删除显著地与 PEPR1LRR 损害了 AtPep1 相互作用。一起,我们的数据由 PEPR1 揭示 AtPep1 识别的保存结构的机制,由他们的血缘的 LRR-RKs 提供重要卓见进另外的肽的识别的预言。 | Jiao Tang Zhifu Han Yadong Sun Heqiao Zhang Xinqi Gong Jijie Chai | 2015 | Cell Research2015，25，1： | 19 |
| 4 | Ligand-triggered de-repression of Arabidopsis heterotrimeric G proteins coupled to immune receptor kinases显示文摘 | Xiangxiu Liang Miaomiao Ma ,Zhaoyang Zhou Jinlong Wang Xinru Yang Shaofei Rao Guozhi Bi Lin Li Xiaojuan Zhang Jijie Chai She Chen Jian-Min Zhou | 2018 | Cell Research2018，28，5： | 13 |
| 5 | Crystal structure of PXY-TDIF complex reveals a conserved recognition mechanism among CLE peptide-receptor pairs显示文摘 | Heqiao Zhang Xiaoya Lin Zhifu Han Li-Jia Qu Jijie Chai | 2016 | Cell Research2016，26，5： | 11 |
| 6 | SERK Family Receptor-like Kinases Function as Co-receptors with PXY for Plant Vascular Development显示文摘 | Heqiao Zhang Xiaoya Lin Zhifu Han Jizong Wang Li-Jia Qu Jijie Chai | 2016 | Molecular Plant2016，9，10： | 11 |
| 7 | Molecular actions of NLR immune receptors in plants and animals显示文摘NLRs constitute intracellular immune receptors in both plants and animals. Direct or indirect ligand recognition results in formation of oligomeric NLR complexes to mediate immune signaling. Over the past 20 years, rapid progress has been made in our understanding of NLR signaling. Structural and biochemical studies provide insight into molecular basis of autoinhibition,ligand recognition, and resistosome/inflammasome formation of several NLRs. In this review, we summarize these studies focusing on the structural aspect of NLRs. We also discuss the analogies and differences between plant and animal NLRs in their mechanisms of action and how the available knowledge may shed light on the signaling mechanisms of other NLRs. | Jizong Wang Jijie Chai | 2020 | Science China(Life Sciences)2020，63，9： | 9 |
| 8 | Apoptosome and inflammasome: conserved machineries for caspase activation显示文摘Apoptosome and inlammasome are multimeric protein complexes that mediate the activation of speciic caspases at the onset of apoptosis and inlammation.he central component of apoptosome or inlammasome is a tripartite scafold protein,exempliied by Apaf-1 and NLRC4,which contains an amino-terminal homotypic interaction motif,a central nucleotide-binding oligomerization domain and a carboxyl-terminal ligand-sensing domain.In the absence of death cue or an inlammatory signal,Apaf-1 or NLRC4 exists in an auto-inhibited,monomeric state,which is stabilized by adenosine diphosphate(ADP).Binding to an apoptosis-or inlammation-inducing ligand,together with replacement of ADP by adenosine triphosphate(ATP),results in the formation of a multimeric apoptosome or inlammasome.he assembled apoptosome and inlammasome serve as dedicated machineries to facilitate the activation of speciic caspases.In this review,we describe the structure and functional mechanisms of mammalian inlammasome and apoptosomes from three representative organisms.Emphasis is placed on the molecular mechanism of caspase activation and the shared features of apoptosomes and inlammasomes. | Jijie Chai Yigong Shi | 2014 | National Science Review2014，1，1： | 6 |
| 9 | Structural basis for differential recognition of brassinolide by its receptors显示文摘Brassinosteroids,a group of plant steroid hormones,reg-ulate 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 identifi ed thus far.Although these studies provide a structural basis for the recognition of brassi-nolide by its receptor BRI1,it still remains poorly under-stood how the hormone differentiates among its con-served 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 effi cient design of plant growth regulators for agricultural practice.On the basis of our structural studies and others’data,we also suggest possible mech-anisms for the activation of BRI1 family receptors. | Ji She Zhifu Han Bin Zhou Jijie Chai | 2013 | Protein & Cell2013，4，6： | 6 |
| 10 | Crystal structure of a TALE protein reveals an extended N-terminal DNA binding region显示文摘 | Haishan Gao Xiaojing Wu Jijie Chai Zhifu Han | 2012 | Cell Research2012，22，12： | 4 |
| 11 | Structural basis for specific self-incompatibility response in Brassica显示文摘自我障碍(SI ) 是在阻止自体受精的 flowering 植物的普遍机制并且使近交。在 Brassica,高度多态的 S 地点充满半胱氨酸的蛋白质的识别(SCR;或 S 地点蛋白质 11 ) 由同样多态的 S 地点受体, kinase (SRK ) 支配 SI 特性。这里,我们从 Brassica rapa 与 SCR9 在建筑群报导 SRK9 (eSRK9 ) 的细胞外的领域的水晶结构。SCR9 绑定导致 eSRK9 homodimerization,形成 2:2 eSRK : 有象信 A 一样的形状的 SCR heterotetramer。SCR9 的特定的识别通过三超(hv ) 被调停 eSRK9 的区域。每 SCR9 同时从第二 eSRK9 单体从一 eSRK9 单体和 hvII 的另外的一半与 hvII 的 hvI 和一个一半交往,起在调停的一个主要作用没有包含在二个 SCR9 分子之间的相互作用的 SRK9 homodimerization。为 eSRK9-SCR9 相互作用批评的残余的单个变化在 vitro 破坏他们的绑定。我们的学习文饰由 SRK 的 SCR 的特定的识别上的数据的身体并且为理解在 SRK 和 SCR 之间的合作进化提供一个结构的模板。 | Rui Ma Zhifu Han Zehan Hu Guangzhong Lin Xinqi Gong Heqiao Zhang June B Nasrallah Jijie Chai | 2016 | Cell Research2016，26，12： | 3 |
| 12 | Structural basis for specific flagellin recognition by t ~ILR protein NAIP5显示文摘充满域的核苷酸绑定和包含蛋白质(NLR ) 的充满白氨酸的重复(LRR ) 作为细胞内部的有免疫力的受体工作检测导出病原体或导出主人的信号的存在。NLR 怎么察觉到他们的 ligands 的机制留下逃犯。这里,我们与 cryo 电子显微镜学在 4.28 点决定的 NLR 蛋白质 NAIP5 和 NLRC4 在建筑群报导细菌的 flagellin 衍生物的结构吗?分辨率。结构表明 flagellin 衍生物形成包括 NAIP5 的 BIR1 和 LRR 与多重领域交往的二平行 helices。对在 flagellin 衍生物的将近完全的埋葬的 NAIP5 结果有约束力,因此稳定 NAIP5 的活跃符合构造。flagellin 的极端 C 终端方面被抛锚到 NAIP5 的一个位地抑制的有约束力的衣袋,它多半由 NAIP5 为不同细菌的 flagellins 的辨别充当一个结构的决定因素,一个观点进一步由生物化学的数据支持了。一起拿,我们的结果使位于 NLR ligand 下面的分子的机制清楚些感觉。 | Xinru Yang Fan Yang Weiguang Wang Guangzhong Lin Zehan Hu Zhifu Han Yijun Qi Liman Zhang Jiawei Wang Sen-Fang Sui Jijie Chai | 2018 | Cell Research2018，28，1： | 2 |
| 13 | Structural Insight into Recognition of Plant Peptid Hormones by Receptors显示文摘分泌的发信号的肽或肽荷尔蒙通过房间房间通讯的协作在植物生长和开发起关键作用。在植物的肽荷尔蒙的感觉通常依靠膜局部性的受体 kinases (RK ) 。进步最近在在 posttranslationally 修改的肽荷尔蒙和 RK 之间的相互作用的结构的说明被取得了。结构的研究建议保存受体绑定和包含他们的保存 C 终点的这类肽荷尔蒙的激活机制。这里,我们考察这些结构的数据并且讨论保存机制怎么能被用来匹配 peptide-RK 对。 | Heqiao Zhang Zhifu Han Wen Song Jijie Chai | 2016 | Molecular Plant2016，9，11： | 2 |
| 14 | Crystal 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 | 2014 | Science China(Life Sciences)2014，57，1： | 2 |
| 15 | Structural basis for BIRl-mediated negative regulation of plant immunity显示文摘 | Cuiyan Ma Yanan Liu Bing Bai Zhifu Han Jiao Tang Heqiao Zhang Hoda Yaghmaiean Yuelin Zhang Jijie Chai | 2017 | Cell Research2017，27，12： | 2 |
| 16 | Crystal structure of an LRR protein with two solenoids显示文摘 | Peiyuan Liu Zehan Hu Bin Zhou Simiao Liu Jijie Chai | 2013 | Cell Research2013，23，2： | 2 |
| 17 | Structure, biochemical function, and signaling mechanism of plant NLRs显示文摘To counter pathogen invasion,plants have evolved a large number of immune receptors,including membrane-resident pattern recognition receptors(PRRs)and intracellular nucleotide-binding and leucine-rich repeat receptors(NLRs).Our knowledge about PRR and NLR signaling mechanisms has expanded significantly over the past few years.Plant NLRs form multi-protein complexes called resistosomes in response to pathogen effectors,and the signaling mediated by NLR resistosomes converges on Ca2+-permeable channels.Ca2+-permeable channels important for PRR signaling have also been identified.These findings highlight a crucial role of Ca2+in triggering plant immune signaling.In this review,we first discuss the structural and biochemical mechanisms of non-canonical NLR Ca2+channels and then summarize our knowledge about immune-related Ca2+-permeable channels and their roles in PRR and NLR signaling.We also discuss the potential role of Ca2+in the intricate interaction between PRR and NLR signaling. | Jizong Wang Wen Song Jijie Chai | 2023 | Molecular Plant2023，16，1： | 1 |
| 18 | Structural basis for a homodimeric ATPase subunit of an ECF transporter显示文摘The transition metal cobalt,an essential cofactor for many enzymes in prokaryotes,is taken up by several specifi c transport systems.The CbiMNQO protein complex be-longs to type-1 energy-coupling factor(ECF)transporters and is a widespread group of microbial cobalt transport-ers.CbiO is the ATPase subunit(A-component)of the cobalt transporting system in the gram-negative thermo-philic bacterium Thermoanaerobacter tengcongensis.Here we report the crystal structure of a nucleotide-free CbiO at a resolution of 2.3Å.CbiO contains an N-terminal canonical nucleotide-binding domain(NBD)and C-termi-nal helical domain.Structural and biochemical data show that CbiO forms a homodimer mediated by the NBD and the C-terminal domain.Interactions mainly via conserved hydrophobic amino acids between the two C-terminal do-mains result in formation of a four-helix bundle.Structural comparison with other ECF transporters suggests that non-conserved residues outside the T-component bind-ing groove in the A component likely act as a specifi city determinant for T components.Together,our data provide information on understanding of the structural organiza-tion and interaction of the CbiMNQO system. | Chengliang Chai You Yu Wei Zhuo Haifeng Zhao Xiaolu Li Na Wang Jijie Chai Maojun Yang | 2013 | Protein & Cell2013，4，10： | 1 |
| 19 | Structural and biochemical basis of apoptosic activation by Smac/DIABLO显示文摘 | Jijie Chai Chunying DU Jia WW | 2000 | Nature2000，406，： | 1 |
| 20 | A loop matters for FTO substrate selection显示文摘Recent studies have unequivocally established the link between FTO and obesity.FTO was biochemically shown to belong to the AlkB-like family DNA/RNA demethylase.However,FTO differs from other AlkB members in that it has unique substrate specificity and contains an extended C-terminus with unknown functions.Insight into the substrate selection mechanism and a functional clue to the C-terminus of FTO were gained from recent structural and biochemical studies.These data would be valuable to design FTO-specific inhibitors that can be potentially translated into therapeutic agents for treatment of obesity or obesity-related diseases. | Zhifu Han Ning Huang Tianhui Niu Jijie Chai | 2010 | Protein & Cell2010，1，7： | 1 |
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