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Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor
TLDR
Three different crystal structures of the extracellular ligand-binding region of mGluR1 are determined—in a complex with glutamate and in two unliganded forms, implying that glutamate binding stabilizes both the ‘active’ dimer and the ’closed’ protomer in dynamic equilibrium. Expand
Structures of the extracellular regions of the group II/III metabotropic glutamate receptors
TLDR
A general activation mechanism of the dimeric receptor coupled with both ligand-binding and interprotomer rearrangements is proposed and revealed the lateral interaction between the two cysteine-rich domains, which could stimulate clustering of theDimeric receptors on the cell surface. Expand
Structural and functional studies of MinD ATPase: implications for the molecular recognition of the bacterial cell division apparatus
TLDR
The results suggest that the residues around the ATP‐binding site are required for the direct interaction with MinC, and that ATP binding and hydrolysis play a role as a molecular switch to control the mechanisms of MinCDE‐dependent bacterial cell division. Expand
Structural views of the ligand-binding cores of a metabotropic glutamate receptor complexed with an antagonist and both glutamate and Gd3+
TLDR
The structural comparison between the active and resting dimers suggests that glutamate binding tends to induce domain closing and a small shift of a helix in the dimer interface, and an interprotomer contact including the acidic patch inhibited dimer formation by the two open protomers in the active state. Expand
CENP-T-W-S-X Forms a Unique Centromeric Chromatin Structure with a Histone-like Fold
TLDR
The data suggest that the CENP-T-W-S-X complex forms a unique nucleosome-like structure to generate contacts with DNA, extending the "histone code" beyond canonicalucleosome proteins. Expand
Atomic structure of the RuvC resolvase: A holliday junction-specific endonuclease from E. coli
TLDR
The crystal structure of the RuvC protein, a Holliday junction resolvase from E. coli, has been determined at 2.5 A resolution and reveals that the catalytic center lies at the bottom of a cleft that nicely fits a DNA duplex. Expand
Structure of the whole cytosolic region of ATP-dependent protease FtsH.
TLDR
Here the authors present two crystal structures: the protease domain and the whole cytosolic region, which fully retains an ATP-dependent protease activity and adopts a three-fold-symmetric hexameric structure. Expand
Integrated molecular mechanism directing nucleosome reorganization by human FACT.
TLDR
Structural and biochemical studies of human FACT-histone interactions present precise views of nucleosome reorganization, conducted by the F ACT-SPT16 (suppressor of Ty 16) Mid domain and its adjacent acidic AID segment. Expand
Crystal structure of the holliday junction DNA in complex with a single RuvA tetramer.
TLDR
The solved crystal structure of the Holliday junction bound to a single Escherichia coli RuvA tetramer at 3.1-A resolution revealed an open concave architecture with a four-fold symmetry, which suggests a possible scheme for successive base pair rearrangements, which may account for smooth Holliday Junction movement without segmental unwinding. Expand
Solution structure of the DNA- and RPA-binding domain of the human repair factor XPA
The solution structure of the central domain of the human nucleotide excision repair protein XPA, which binds to damaged DNA and replication protein A (RPA), was determined by nuclear magneticExpand
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