The WRKY proteins are a family of plant-specific transcription factors(TFs)that are widely involved in plant development and anti-stress responses.Arabidopsis WRKY11(AtWRKY11)functions in regulating plant defense agai...The WRKY proteins are a family of plant-specific transcription factors(TFs)that are widely involved in plant development and anti-stress responses.Arabidopsis WRKY11(AtWRKY11)functions in regulating plant defense against abiotic stress and belongs to the Ild subgroup of WRKY TFs.We herein report the expres sion,purification and preliminary structural characterization of AtWRKY11 DNA-binding domain(DBD)using solution NMR Almost complete backbone chemical shift assignments of AtWRKY11-DBD have been ob-tained.Chemical shift-based secondary structure analysis suggests that AtWRKY11-DBD may exhibit local conformational diferences from the X-ray structure of the C-terminal WRKY domain of AtWRKY1,particularly in the β1 and β5 strands.Our current study provides the basis for further structural and interactional studies.展开更多
G-protein-coupled receptors(GPCRs)mediate a wide range of cellular responses to various ligands or stimuli,and are the most important drug targets associated with human diseases.While major advances in GPCR structural...G-protein-coupled receptors(GPCRs)mediate a wide range of cellular responses to various ligands or stimuli,and are the most important drug targets associated with human diseases.While major advances in GPCR structural biology have greatly deepened our understanding of its activation mechanism,the highly complex changes in the structural dynamics of GPCRs during activation remain underdetermined and their links to physiological functions largely unknown.Solution nuclear magnetic resonance(NMR)spectroscopy is an essential technique that allows the characterization of protein structural dynamics at atomic level,and has been applied in the studies of GPCR structural-function relationship in the past decade.Herein,we summarize a few specific studies in which solution NMR methods were employed and provided novel insights into questions difficult to be addressed by other methods.展开更多
Molecular chaperones are diverse families of proteins that play key roles in protein homeostasis.They assist the folding of client proteins or prevent them from rreversible aggregation under stress conditions.Diverse ...Molecular chaperones are diverse families of proteins that play key roles in protein homeostasis.They assist the folding of client proteins or prevent them from rreversible aggregation under stress conditions.Diverse chaper-one families contribute to different aspects of protein homeostasis by inter-acting with a wide range of client proteins.Despite the vital roles of chaper-ones in cell survival,the molecular mechanisms underlying chaperone func-tions remain elusive,due to the non-specificity of chaperone-client interac-tions and the intrinsic flexibility of the clients.展开更多
基金This work was supported by grants 2018YFE0202300,2018YFA0704002 from the National Key R&D Program of Chinagrant 21735007 from the National Natural Science Foundation of China to M.L.grant 21991083 from the National Natural Science Foundation of China to Y.H.
文摘The WRKY proteins are a family of plant-specific transcription factors(TFs)that are widely involved in plant development and anti-stress responses.Arabidopsis WRKY11(AtWRKY11)functions in regulating plant defense against abiotic stress and belongs to the Ild subgroup of WRKY TFs.We herein report the expres sion,purification and preliminary structural characterization of AtWRKY11 DNA-binding domain(DBD)using solution NMR Almost complete backbone chemical shift assignments of AtWRKY11-DBD have been ob-tained.Chemical shift-based secondary structure analysis suggests that AtWRKY11-DBD may exhibit local conformational diferences from the X-ray structure of the C-terminal WRKY domain of AtWRKY1,particularly in the β1 and β5 strands.Our current study provides the basis for further structural and interactional studies.
文摘G-protein-coupled receptors(GPCRs)mediate a wide range of cellular responses to various ligands or stimuli,and are the most important drug targets associated with human diseases.While major advances in GPCR structural biology have greatly deepened our understanding of its activation mechanism,the highly complex changes in the structural dynamics of GPCRs during activation remain underdetermined and their links to physiological functions largely unknown.Solution nuclear magnetic resonance(NMR)spectroscopy is an essential technique that allows the characterization of protein structural dynamics at atomic level,and has been applied in the studies of GPCR structural-function relationship in the past decade.Herein,we summarize a few specific studies in which solution NMR methods were employed and provided novel insights into questions difficult to be addressed by other methods.
基金This work is supported by grants from the National Key R&D Program of China(Nos.2018YFA0704002,2018YFE0202300,2017YFA0505400)the Natlonal Natural sclence Foundatlon uf China(Nos.21735007,21675170,21475146,31370718)the Chinese Academy of Sciences(No.QYZDJ-SSW-SLH027).
文摘Molecular chaperones are diverse families of proteins that play key roles in protein homeostasis.They assist the folding of client proteins or prevent them from rreversible aggregation under stress conditions.Diverse chaper-one families contribute to different aspects of protein homeostasis by inter-acting with a wide range of client proteins.Despite the vital roles of chaper-ones in cell survival,the molecular mechanisms underlying chaperone func-tions remain elusive,due to the non-specificity of chaperone-client interac-tions and the intrinsic flexibility of the clients.
