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Changwen Jin
Peking University
Molecular biologyChemistryEscherichia coliBiochemistryBiology
116Publications
21H-index
1,646Citations
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Publications 110
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#1Xiaogang Niu (PKU: Peking University)H-Index: 3
#2Shuaipeng Ma (PKU: Peking University)
Last. Changwen JinH-Index: 21
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The 26S proteasome degrades selected polyubiquitinated proteins in the ubiquitin–proteasome system, which is the major pathway for programmed protein degradation in eukaryotic cells. The Saccharomyces cerevisiae Rpn12 locates in the lid of the 19S regulatory particle within the 26S proteasome and plays a role in recruiting the extrinsic ubiquitin receptor Rpn10. Rpn12 contains a N-terminal TPR (tetratrico peptide repeat)-like domain and a C-terminal WH (winged helix) domain. Interaction of Rpn12...
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#1Qi Liu (CAS: Chinese Academy of Sciences)
#1Qi Liu (CAS: Chinese Academy of Sciences)
Last. Jin-Peng Sun (PKU: Peking University)H-Index: 17
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Characterization of the dynamic conformational changes in membrane protein signaling complexes by nuclear magnetic resonance (NMR) spectroscopy remains challenging. Here, we developed "DeSipher" technology to site-specifically incorporate 4-trimethylsilyl phenylalanine (TMSiPhe) into proteins and measured the conformational changes in the signaling complex by 1H NMR. Notably, crystallographic analysis revealed structural changes that reshaped the TMSiPhe-specific amino-acyl tRNA synthetase to ac...
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#1Jun Xu (THU: Tsinghua University)H-Index: 3
#2Yunfei Hu (PKU: Peking University)H-Index: 12
Last. Brian K. Kobilka (Stanford University)H-Index: 113
view all 11 authors...
Summary The M2 muscarinic acetylcholine receptor (M2R) is a prototypical GPCR that plays important roles in regulating heart rate and CNS functions. Crystal structures provide snapshots of the M2R in inactive and active states, but the allosteric link between the ligand binding pocket and cytoplasmic surface remains poorly understood. Here we used solution NMR to examine the structure and dynamics of the M2R labeled with 13CH3-e-methionine upon binding to various orthosteric and allosteric ligan...
1 CitationsSource
#1Wenbo Zhang (PKU: Peking University)H-Index: 1
#2Cong Zhao (PKU: Peking University)
Last. Changwen Jin (PKU: Peking University)H-Index: 21
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The 26S proteasome is responsible for the selective, ATP-dependent degradation of polyubiquitinated proteins in eukaryotic cells. It consists of a 20S barrel-shaped core particle capped by two 19S regulatory particle at both ends. The Rpn5 subunit is a non-ATPase subunit located in the lid subcomplex of the 19S regulatory particle and is identified to inhibit the Rpn11 deubiquitinase activity in the isolated lid. The protein contains a C-terminal proteasome–CSN–eIF3 (PCI) domain and an N-termina...
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#1Xing-Chi YuH-Index: 1
#2Yunfei HuH-Index: 12
Last. Changwen JinH-Index: 21
view all 5 authors...
1 CitationsSource
#1Moye Jia (PKU: Peking University)
#2Yunfei Hu (PKU: Peking University)H-Index: 12
Last. Changwen Jin (PKU: Peking University)H-Index: 21
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The periplasmic chaperone SurA in Gram-negative bacteria plays a central role in the biogenesis of integral outer membrane proteins and is critical to the maintenance of bacterial membrane integrity. SurA contains a core chaperone module comprising the N- and C-terminal domains, along with two peptidyl-prolyl isomerase (PPIase) domains. The chaperone activity of SurA has been demonstrated to rely on the core module, whereas recent works suggested that the PPIase domains may regulate the chaperon...
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#1Wenbo Zhang (PKU: Peking University)H-Index: 1
#2Xiaogang Niu (PKU: Peking University)H-Index: 3
Last. Changwen JinH-Index: 21
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The thioredoxin (Trx)-coupled arsenate reductase (ArsC) is a family of enzymes that catalyzes the reduction of arsenate to arsenite in the arsenic detoxification pathway. The catalytic cycle involves a series of relayed intramolecular and intermolecular thiol-disulfide exchange reactions. Structures at different reaction stages have been determined, suggesting significant conformational fluctuations along the reaction pathway. Herein, we use two state-of-the-art NMR methods, the chemical exchang...
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#1Wenbo Zhang (PKU: Peking University)H-Index: 1
#2Cong Zhao (PKU: Peking University)
Last. Changwen JinH-Index: 21
view all 4 authors...
Abstract The 26S proteasome is the major protein degradation machinery in living cells. The Rpn5 protein is one scaffolding subunit in the lid subcomplex of the 19S regulatory particle in the proteasome holoenzyme. Herein we report the solution structure of the N-terminal domain (NTD) of yeast Rpn5 at high resolution by NMR spectroscopy. The results show that Rpn5 NTD adopts α-solenoid-like fold in right-handed superhelical configuration formed by a number of α-helices. Structural comparisons wi...
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