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Skelemin association with ?IIb?3 integrin: a structural model.

ABSTRACT: 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 ?IIb?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.

SUBMITTER: Gorbatyuk V

PROVIDER: S-EPMC4222533 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature

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Skelemin association with αIIbβ3 integrin: a structural model.

Gorbatyuk Vitaliy V Nguyen Khiem K Podolnikova Nataly P NP Deshmukh Lalit L Lin Xiaochen X Ugarova Tatiana P TP Vinogradova Olga O

Biochemistry 20141022 43

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 αIIbβ3. The model of tertiary assem ...[more]

PMID: 25224262

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