Recognition Sites of RGD-Dependent Integrins

  • Martin Pfaff

Abstract

The tripeptide motif Arg-Gly-Asp (RGD) was identified more than 12 years ago as a minimal essential peptide sequence inhibiting cell adhesion to fibronectin.1–3 Subsequently, short RGD-peptides were found to inhibit the binding of other major cell-adhesive proteins like vitronectin, fibrinogen or van Willebrand factor, indicating the central biological importance of this simple peptide motif as the basic unit of a widespread cellular recognition system.4–7 In the last 10 years, with the rapid accumulation of available protein sequence information and the discovery of various families of adhesion receptors, these initial findings have been corroborated.8,9 However, apart from RGD, other important cell adhesion motifs have been identified and we know today that cell adhesion to an extracellular matrix protein can involve a series of different receptor-ligand interactions. Therefore RGD-recognition is not the unique mechanism for interactions of proteins with cells, but it is unique with respect to its broad distribution in biological organisms and its usage by a large number of different cell-adhesive proteins and cell-adhesion receptors.

Keywords

Osteoporosis Glycine Immobilization Proline Alanine 

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© Springer Science+Business Media Dordrecht 1997

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  • Martin Pfaff

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