Collagen XXII binds to collagen-binding integrins via the novel motifs GLQGER and GFKGER.
BIOCHEMICAL JOURNAL(2014)
摘要
Collagen XXII, a FACIT (fibril-associated collagen with interrupted triple helices), is expressed at the myotendinous junction and the articular surface of joint cartilage. Cellular receptors like collagen-binding integrins are known to bind collagens with distinct binding motifs following the sequence GXOGER. In the present study, we demonstrate the sequences GLQGER and GFKGER as novel binding motifs between collagen XXII and collagen-binding integrins, especially alpha 2 beta 1 integrin. Solid-phase assays and surface plasmon resonance spectroscopy revealed a direct interaction between alpha 2 beta 1 integrin and the motif GFKGER. In addition, immunohistochemical analysis demonstrated partial co-localization of collagen XXII, alpha 2 beta 1 integrin and alpha 11 beta 1 integrin at the myotendinous junction. Furthermore, computational modelling of the motifs GLQGER and GFKGER showed perfect fitting of the sequences into the binding pocket of collagen-binding integrins. Taken together, we demonstrated that collagen XXII interacts with collagen-binding integrins via the new motifs GLQGER and GFKGER.
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关键词
binding motif,collagen-binding integrin,extracellular matrix,fibril-associated collagen with interrupted triple helices (FACIT),hexapeptide
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