The Three-Dimensional Structure of the RGD (Arg-Gly-Asp) Adhesion Sequence of Fibronectin; NMR Studies of the Peptides RGDS and GRGDSP.
- 1 January 1990
- journal article
- research article
- Published by Danish Chemical Society in Acta Chemica Scandinavica
- Vol. 44 (2) , 161-164
- https://doi.org/10.3891/acta.chem.scand.44-0161
Abstract
The cell adhesion property of fibronectin and a number of proteins with similar properties resides in the RGD-sequence. The NMR spectrum of the active peptide GRGDSP at pH 3.5 shows that the peptide has the same stereostructure as that reported at pH 7.0. NMR mesurements of the smallest active peptide RGDS at pH 3.5 and pH 5, including temperature gradients up to 70.degree. C, reveal similarities with GRGDSP. The NH-protons of aspartic acid and serine are only slowly exchanged indicating their participation in hydrogen bonds, which implies an exceptionally rigid stereostructure.This publication has 1 reference indexed in Scilit:
- Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion.Journal of Biological Chemistry, 1987