Identification of the Arg‐Gly‐Asp sequence in laminin A chain as a latent cell‐binding site being exposed in fragment P1
- 12 March 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 262 (1) , 82-86
- https://doi.org/10.1016/0014-5793(90)80159-g
Abstract
A single RGD-containing sequence present within an epidermal growth factor-like repeat of the short arms of laminin is shown by peptide inhibition to block integrin receptors recognizing a latent cell-binding site of laminin. Based on proteolysis data it is proposed that masking occurs by folding of the globular domain IVa over the cell-binding site in the adjacent rod-like structures of laminin A chain.Keywords
This publication has 28 references indexed in Scilit:
- EGF‐like domains in extracellular matrix proteins: Localized signals for growth and differentiation?FEBS Letters, 1989
- Structure and biological activity of basement membrane proteinsEuropean Journal of Biochemistry, 1989
- The high‐affinity binding of laminin to cellsEuropean Journal of Biochemistry, 1989
- Domains of laminin with growth-factor activityCell, 1989
- FIBRONECTIN AND ITS RECEPTORSAnnual Review of Biochemistry, 1988
- Laminin-nidogen complex. Extraction with chelating agents and structural characterizationEuropean Journal of Biochemistry, 1987
- Integrins: A family of cell surface receptorsCell, 1987
- Characterization of a laminin receptor from human breast carcinoma tissueBreast Cancer Research and Treatment, 1984
- Protease Resistance and Conformation of LamininEuropean Journal of Biochemistry, 1982
- Shapes, domain organizations and flexibility of laminin and fibronectin, two multifunctional proteins of the extracellular matrixJournal of Molecular Biology, 1981