Unique charge-dependent constraint on collagen recognition by integrin α10β1

@inproceedings{Hamaia2017UniqueCC,
  title={Unique charge-dependent constraint on collagen recognition by integrin α10β1},
  author={Samir W. Hamaia and Daisy Luff and Emma J. Hunter and Jean-Daniel M. Malcor and Dominique G. Bihan and Donald Gullberg and Richard W Farndale},
  booktitle={Matrix biology : journal of the International Society for Matrix Biology},
  year={2017}
}
The collagen-binding integrins recognise collagen through their inserted (I) domain, where co-ordination of a Mg2+ ion in the metal ion-dependent site is reorganised by ligation by a collagen glutamate residue found in specific collagen hexapeptide motifs. Here we show that GROGER, found in the N-terminal domain of collagens I and III, is only weakly recognised by α10β1, an important collagen receptor on chondrocytes, contrasting with the other collagen-binding integrins. Alignment of I domain… CONTINUE READING