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Over the last two decades, our knowledge concerning intracellular events that regulate integrin’s affinity to their soluble ligands has significantly improved. However, the mechanism of adhesion-induced integrin clustering and development

Over the last two decades, our knowledge concerning intracellular events that regulate integrin’s affinity to their soluble ligands has significantly improved. However, the mechanism of adhesion-induced integrin clustering and development of focal complexes, which could further mature to form focal adhesions, still remains under-investigated. Here we present a structural model of tandem IgC2 domains of skelemin in complex with the cytoplasmic tails of integrin α[subscript IIb]β[subscript 3].

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Date Created
  • 2014-11-04
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  • Text
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    Identifier
    • Digital object identifier: 10.1021/bi500680s
    • Identifier Type
      International standard serial number
      Identifier Value
      0006-2960
    • Identifier Type
      International standard serial number
      Identifier Value
      1520-4995
    Note
    • This document is the Accepted Manuscript version of a Published Work that appeared in final form in BIOCHEMISTRY, copyright American Chemical Society, after peer review and technical editing by the publisher. To access the final published work, see http://dx.doi.org/10.1021/bi500680s, opens in a new window

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    Gorbatyuk, Vitaliy, Khiem Nguyen, Podolnikova, Nataly P., Deshmukh, Lalit, Lin, Xiaochen, Ugarova, Tatiana P., & Vinogradova, Olga (2014). Skelemin Association with alpha(IIb)beta(3) Integrin: A Structural Model. BIOCHEMISTRY, 53(43), 6766-6775. http://dx.doi.org/10.1021/bi500680s

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