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Crystal structure of the RNA-guided immune surveillance Cascade complex in Escherichia coli
The structure of the Cascade complex provides novel molecular details of protein–protein and protein–RNA alignments and interactions required for generation of a complex mediating RNA-guided immune surveillance and explains why the seed sequence has a critical role in target DNA recognition.
Crystal structures of the extracellular domain of LRP6 and its complex with DKK1
- Z. Cheng, T. Biechele, +4 authors W. Xu
- Biology, MedicineNature Structural &Molecular Biology
- 1 November 2011
Crystal structures of a human LRP6-E3E4–DKK1 complex and the first and second halves of human L RP6's four propeller–epidermal growth factor (EGF) pairs are presented to provide key insights for understanding LRP5/6 structure and the interaction of LRP 5/6 with DKK, as well as for drug discovery.
Domain‐swapped dimerization of ZO‐1 PDZ2 generates specific and regulatory connexin43‐binding sites
- Jia Chen, L. Pan, Zhiyi Wei, Yanxiang Zhao, Mingjie Zhang
- Biology, MedicineThe EMBO journal
- 6 August 2008
It is demonstrated that the domain‐swapped dimerization of zonula occludens‐1 PDZ2 generates a distinct interface that functions together with the well‐separated canonical carboxyl tail‐binding pocket in each PDZ unit in binding to connexin43 (Cx43).
Structure of MyTH4-FERM Domains in Myosin VIIa Tail Bound to Cargo
The crystal structure of MYO7A MyTH4-FERM domains in complex with the central domain (CEN) of Sans at 2.8 angstrom resolution is reported, providing mechanistic explanations for known deafness-causing mutations in MYO8A Myth4-FerM.
Structure of Crumbs tail in complex with the PALS1 PDZ–SH3–GK tandem reveals a highly specific assembly mechanism for the apical Crumbs complex
- Youjun Li, Zhiyi Wei, Yan Yan, Qingwen Wan, Q. Du, Mingjie Zhang
- Biology, MedicineProceedings of the National Academy of Sciences
- 10 November 2014
It is discovered that the PDZ–SH3–GK tandem of PALS1 forms a structural supramodule interacting with the large part of the Crumbs tail with high affinity and specificity, supporting the apical–basal polarity of epithelial cells.
Structural Basis for the Phosphorylation-regulated Interaction between the Cytoplasmic Tail of Cell Polarity Protein Crumbs and the Actin-binding Protein Moesin*
- Zhiyi Wei, Youjun Li, F. Ye, Mingjie Zhang
- Biology, MedicineThe Journal of Biological Chemistry
- 19 March 2015
PKC can actively prevent the Crb·moesin complex formation and thereby shift Crb to form complex with PALS1 at apical junctions, indicating that Crb may serve as an aPKC-mediated sensor in coordinating contact-dependent cell growth inhibition in epithelial tissues.
Autoinhibition of UNC5b revealed by the cytoplasmic domain structure of the receptor.
The crystal structure of the cytoplasmic portion of UNC5b is determined, finding that it contains three distinctly folded domains, namely ZU5, UPA, and death domain (DD), which form a structural supramodule that leads to the activation of the receptor in the promotion of apoptosis and blood vessel patterning.
Crystal structures of E. coli laccase CueO at different copper concentrations.
- Xu Li, Zhiyi Wei, +4 authors W. Gong
- Chemistry, MedicineBiochemical and biophysical research…
- 2 March 2007
Structural comparison between CueO and other three fungal laccase proteins indicates that Glu106 in CueO constitutes the primary counter-work for reconstitution of the trinuclear copper site and supports the copper dependence of CueO oxidase activity.
LGN/mInsc and LGN/NuMA complex structures suggest distinct functions in asymmetric cell division for the Par3/mInsc/LGN and Gαi/LGN/NuMA pathways.
The results suggest that the Par3/mInsc/LGN and NuMA/L GN/Gαi complexes play sequential and partially overlapping roles in asymmetric cell division.
Myosin VI Undergoes Cargo-Mediated Dimerization
The high-resolution NMR structure of the cargo-free myosin VI cargo-binding domain (CBD) is reported and it is shown that it is a stable monomer in solution and may represent a general paradigm for the regulation of processivity for myOSin VI as well as other myosins, including myosIn VII and myos in X.