Nihon Kessho Gakkaishi
Online ISSN : 1884-5576
Print ISSN : 0369-4585
ISSN-L : 0369-4585
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Volume 54, Issue 4
Displaying 1-13 of 13 articles from this issue
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Review Article
Articles
  • Recognition Mechanism of the Cell Polarity Protein Mammalian Inscuteable-LGN Complex
    Satoru YUZAWA
    2012Volume 54Issue 4 Pages 206-212
    Published: August 31, 2012
    Released on J-STAGE: September 06, 2012
    DOIhttps://doi.org/10.5940/jcrsj.54.206
    JOURNAL FREE ACCESS
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    Interaction between the mammalian cell polarity proteins Inscuteable (mInsc) and LGN plays crucial roles in mitotic spindle orientation, a process contributing to asymmetric cell division. We describe here the crystal structure of the LGN-binding domain (LBD) of human mInsc in complex with the N-terminal TPR domain of human LGN at 2.6 Å resolution. mInsc-LBD adopts an elongated structure containing an α-helix and an antiparallel β-sheet linked by an extended region and runs antiparallel to LGN along the concave surface of the superhelix formed by the TPR motifs, indicative of a novel mode for TPR interaction. Characteristics of interaction between LGN TPR domain and other partner molecules are discussed.
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  • Mechanism for tRNA Agmatinylation Revealed by X-ray Crystallography
    Tomoyuki NUMATA, Takuo OSAWA
    2012Volume 54Issue 4 Pages 213-219
    Published: August 31, 2012
    Released on J-STAGE: September 06, 2012
    DOIhttps://doi.org/10.5940/jcrsj.54.213
    JOURNAL FREE ACCESS
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    The cytidine at the first position of the anticodon (C34) in the AUA codon-specific archaeal tRNAIle2 is modified to 2-agmatinylcytidine (agm2C), which is crucial for the precise decoding of the genetic code. This modification is catalyzed by tRNAIle-agm2C synthetase (TiaS), using ATP and agmatine as substrates. We have determined the crystal structures of TiaS-tRNAIle2 complexed with ATP, or with AMPcPP and agmatine, revealing a novel kinase module requisite for activating C34 by phosphorylation. These structures showed that agmatine is essential for placing C34 in the active site. We also revealed the molecular mechanism by which TiaS discriminates tRNAIle2 from other tRNAs.
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  • Crystal Structure of Channelrhodopsin, A Light-Gated Cation Channel
    Hideaki KATO, Osamu NUREKI
    2012Volume 54Issue 4 Pages 220-225
    Published: August 31, 2012
    Released on J-STAGE: September 06, 2012
    DOIhttps://doi.org/10.5940/jcrsj.54.220
    JOURNAL FREE ACCESS
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    Channelrhodopsin (ChR) is a light-gated cation channel derived from algae that conducts cations, including sodium ions, in a light-dependent manner. Because the inward flow of sodium ions triggers the neuron firing, neurons expressing ChRs can be optically controlled even within freely moving mammals. Although ChR has been broadly applied to neuroscience research, little is known about its molecular mechanisms. We determined the crystal structure of ChR at 2.3 Å resolution and revealed its molecular architecture, especially, the cation-conducting pathway. The integration of structural and electrophysiological analyses provided insight into the molecular basis for the remarkable function of ChR, and paved the way for the principled design of ChR variants with novel properties.
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  • Ferroelectric Phase Transition and Material Property Studies Using State-of-the-Art First-Principles Calculations
    Hiroki MORIWAKE
    2012Volume 54Issue 4 Pages 226-231
    Published: August 31, 2012
    Released on J-STAGE: September 06, 2012
    DOIhttps://doi.org/10.5940/jcrsj.54.226
    JOURNAL FREE ACCESS
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    Ferroelectric material studies, e.g., ferroelectric phase transition of BaTiO3, and CdTiO3, those involving soft-mode phonon, ferroelectric structure and, its materials properties using state-of-the-art first-principles calculations are described.
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