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]. The model of tertiary assembly is generated based upon NMR data and illuminates a potential link between the essential cell adhesion receptors and myosin filaments. This connection may serve as a basis for generating the mechanical forces necessary for cell migration and remodeling.
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- Skelemin Association With Alpha(IIb)Beta(3) Integrin: A Structural Model
- Gorbatyuk, Vitaliy (Author)
- Nguyen, Kheim (Author)
- Podolnikova, Nataly (Author)
- Deshmukh, Lalit (Author)
- Lin, Xiaochen (Author)
- Ugarova, Tatiana (Author)
- Vinogradova, Olga (Author)
- College of Health Solutions (Contributor)
- Digital object identifier: 10.1021/bi500680s
- Identifier TypeInternational standard serial numberIdentifier Value0006-2960
- Identifier TypeInternational standard serial numberIdentifier Value1520-4995
- 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