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Zoology and wildlife conservation

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Abstracts » Zoology and wildlife conservation

Crystal structure of a PDZ domain

Article Abstract:

The recombinant form of the third PDZ domain of the human homolog of Drosophila discs-large tumor-suppressor gene product, DlgA, comprises a 5-stranded antiparallel beta-barrel surrounded by three alpha-helices. The domain's crystal structure includes a groove over its surface, which ends in a conserved hydrophobic pocket with arginine. This pocket is the binding site for the C-terminal peptide. PDZ domains are residue repeats located in a number of proteins. They help in ion-channel and receptor clustering, and linking of receptors to effector enzymes.

Author: Liddington, Robert C., Petosa, Carlo, Poy, Florence, Sutcliffe, Michael J., Cabral, Joao H. Morais, Raza, Sami, Byron, Olwyn, Marfatia, Shirin M., Chishti, Athar H.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
Analysis, Protein structure, Recombinant proteins

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Crystal structure of the breakage-reunion domain of DNA gyrase

Article Abstract:

Researchers have been able to determine the crystal structure of the 'breakage-reunion' domain of the DNA gyrase at 2.8 angstrom resolution. The structure of this 59K (relative molecular mass, 59,000) domain was compared with that of a 92K fragment of yeast topoisomerase II. The structures indicate how it may be possible for the T segment to exit from the bottom of the molecule through the 'primary' dimer interface after passing through the G segment.

Author: Liddington, Robert C., Jackson, Andrew P., Cabral, Joao H. Morais, Smith, Clare V., Shikotra, Nita, Maxwell, Anthony
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
DNA repair, DNA topoisomerase II

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Structure of importin-Beta bound to the IBB domain of importin-alpha

Article Abstract:

The crystal structure of human importin-Beta bound to the IBB domain of human importin-alpha has been solve. The association occurs via combined specific-sequence recognition and gross electrostatic complementarity. The structure provides an indication as to how the binding of Ran-GTP to importin-Beta could result in IBB dissociation, and provides support for the hypothesis that importins alpha and beta have a common ancestor.

Author: Petosa, Carlo, Muller, Christoph W., Cingolani, Gino, Weis, Karsetn
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
Cytosol

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Subjects list: Proteins, Research
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