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   The crystal structure of the Physarum polycephalum actin-fragmin
   kinase: an atypical protein kinase with a specialized substrate-binding
   domain.
   (PMID:10357805)
     * [23]Abstract This article is available in UKPMC
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       by and<br/> those which it cites
     * [25]BioEntities Biological entities annotated by the EMBL EBI and
       NCBI teams
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       words in the title and abstract

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   [28]Steinbacher S,
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   [30]Hof P,
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   [32]Eichinger L,
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   [34]Schleicher M,
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   [36]Gettemans J,
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   [38]Vandekerckhove J,
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   [40]Huber R,
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   [42]Benz J
   Abteilung Strukturforschung, Max-Planck-Institut für Biochemie, 82152
   Martinsried, Germany.
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   [44]The EMBO Journal [1999, 18(11):2923-9]

   Type:  Journal Article, Research Support, Non-U.S. Gov't, Comparative
   Study

   DOI: 10.1093/emboj/18.11.2923 The Digital Object Identifier (DOI)
   System enables identification of digital entities
   Abstract Highlight Terms Highlight biological terms.
   [ ] Gene Ontology(5) [ ] Genes/Proteins(3) [ ] Species(1)

   Coordinated temporal and spatial regulation of the [45]actin
   [46]cytoskeleton is essential for diverse cellular processes such as
   [47]cell division, [48]cell motility and the formation and maintenance
   of specialized structures in differentiated cells. In plasmodia of
   [49]Physarum polycephalum, the F-[50]actin capping activity of the
   [51]actin-fragmin complex is regulated by the [52]phosphorylation of
   [53]actin. This is mediated by a novel type of [54]protein kinase with
   no sequence homology to eukaryotic-type [55]protein kinases. Here we
   present the crystal structure of the catalytic domain of the first

t/data/good/10357805.utf8  view on Meta::CPAN

   residues, in common with the eukaryotic [57]protein kinase superfamily,
   which harbours the [58]nucleotide binding site and the catalytic
   apparatus in an inter-lobe cleft. Several kinases that share this
   catalytic module differ in the overall architecture of their substrate
   recognition domain. The [59]actin-fragmin kinase has acquired a unique
   flat substrate recognition domain which is supposed to confer stringent
   substrate specificity.
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