A5101622975- RNA modifications and cancer
- Enzyme Structure and Function
- Geology and Paleoclimatology Research
- Geochemistry and Elemental Analysis
- PARP inhibition in cancer therapy
- Protein Kinase Regulation and GTPase Signaling
- Biochemical and Molecular Research
- Epigenetics and DNA Methylation
- Geological and Geophysical Studies
- Methane Hydrates and Related Phenomena
- PI3K/AKT/mTOR signaling in cancer
- Geological formations and processes
- Monoclonal and Polyclonal Antibodies Research
- Glycosylation and Glycoproteins Research
- Neonatal Health and Biochemistry
- Plant and Fungal Species Descriptions
- Neuroscience and Neuropharmacology Research
- Cancer-related gene regulation
- Calcium signaling and nucleotide metabolism
- Cell Adhesion Molecules Research
- Histone Deacetylase Inhibitors Research
- Enzyme Production and Characterization
- Ubiquitin and proteasome pathways
- RNA and protein synthesis mechanisms
- Melanoma and MAPK Pathways
Chinese Academy of Sciences
2007-2019
South China Sea Institute Of Oceanology
2015-2019
Institute of Oceanology
2015-2019
University of Chinese Academy of Sciences
2017-2019
Institute of Soil Science
2019
Shanghai Institutes for Biological Sciences
2006-2017
Center for Excellence in Molecular Cell Science
2006-2017
Suzhou Institute of Nano-tech and Nano-bionics
2014
Soochow University
2013
University of Oulu
2012
Rituximab is a widely used monoclonal antibody drug for treating certain lymphomas and autoimmune diseases. To understand the molecular mechanism of recognition human CD20 by Rituximab, we determined crystal structure Fab in complex with synthesized peptide comprising epitope (residues 163-187) at 2.6-A resolution. The combining site consists four complementarity determining regions that form large, deep pocket to accommodate peptide. bound assumes unique cyclic conformation constrained...
The SET- and MYND-domain containing (Smyd) proteins constitute a special subfamily of the SET-containing lysine methyltransferases. Here we present structure full-length human Smyd3 in complex with S-adenosyl-l-homocysteine at 2.8 Å resolution. affords first example that other region(s) besides SET domain its flanking regions participate formation active site. Structural analysis shows previously uncharacterized C-terminal contains tetratrico-peptide repeat (TPR) which together post-SET...
Ras homolog enriched in brain (Rheb), a small GTPase, positively regulates the mTORC1 pathway. The GDP-GTP exchange of Rheb has been suggested to be facilitated by translationally controlled tumor protein (TCTP). Here we demonstrate that human TCTP (hTCTP) interacts with (hRheb) and accelerates its GDP release vitro hTCTP activates pathway vivo. To investigate underlying mechanism, built structure models GDP- GTP-bound hRheb complexes performed molecular dynamics simulations models, which...
The SET- and myeloid-Nervy-DEAF-1 (MYND)-domain containing (Smyd) lysine methyltransferases 1–3 share relatively high sequence similarity but exhibit divergence in the substrate specificity. Here we report crystal structure of full-length human Smyd2 complex with S-adenosyl-L-homocysteine (AdoHcy). Although Smyd1–3 enzymes are similar overall structure, detailed comparisons demonstrate that they differ substantially potential substrate-binding site. binding site Smyd3 consists mainly a deep...
The activity of S6K1 (p70 ribosomal protein subunit 6 kinase 1) is stimulated by phosphorylation Thr389 in the hydrophobic motif mTORC1 (mammalian target rapamycin complex and Thr229 activation loop PDK1 (phosphoinositide-dependent 1); however, order two events still ambiguous. In present paper we report six crystal structures domain alone or plus various forms, complexes with a highly specific inhibitor. structural data, together biochemical reveal vivo absence demonstrate importance...
Isocitrate dehydrogenases (IDHs) catalyze oxidative decarboxylation of isocitrate (ICT) into alpha-ketoglutarate (AKG). We report here the crystal structures Saccharomyces cerevesiae mitochondrial NADP-IDH Idp1p in binary complexes with coenzyme NADP, or substrate ICT, product AKG, and a quaternary complex NADPH, Ca(2+), which represent different enzymatic states during catalytic reaction. Analyses these identify key residues involved binding ligands. Comparisons among previously reported...
HBO1, a member of the MYST family histone acetyltransferases (HATs), is required for global acetylation H3K14 and embryonic development. It functions as catalytic subunit in multisubunit complexes comprising BRPF1/2/3 or JADE1/2/3 scaffold protein, two accessory proteins. BRPF2 has been shown to be important HAT activity HBO1 toward H3K14. Here we demonstrated that can regulate free H3 H4, nucleosomal H3. Particularly, short N-terminal region sufficient binding potentiate its The crystal...
Abstract In molecular self‐assembly molecules form organized structures or patterns. The control of the process is an important and challenging topic. Inspired by cytoskeletal‐membrane protein lipid bilayer system that determines shape eukaryotic cells, we developed a frame‐guided assembly as general strategy to prepare heterovesicles with programmed geometry dimensions. This method offers greater over which may benefit understanding formation mechanism well functions cell membrane.
•Cbln4 interacts with Nrxn1β, forming a stable complex the LNS domain of Nrxn1β•Nrxn1β binds to Cbln1 or Cbln4 likely through strand β10 S4 insert•Loop CD divergence accounts for differences in and binding GluD2•A semiquantitative cell surface assay is developed SummaryUnlike cerebellin 1 (Cbln1), which bridges neurexin (Nrxn) receptors δ-type glutamate trans-synaptic triad, was reported have no weak despite sharing ∼70% sequence identity Cbln1. Here, we report crystal structures homotrimers...
Specific activation of amino acids by aminoacyl-tRNA synthetases is essential for maintaining translational fidelity. Here, we present crystal structures Saccharomyces cerevisiae tryptophanyl-tRNA synthetase (sTrpRS) in apo form and complexes with various ligands. In each complex, there a sulfate ion bound at the active site which mimics α- or β-phosphate group ATP during tryptophan activation. particular, one monomer sTrpRS–TrpNH2O appears to capture snapshot α-phosphate its movement...