title: Identification of the Arg-Gly-Asp sequence in laminin A chain as a latent cell-binding site being exposed in fragment P1.
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.
authors.affiliation: Max-Planck-Institut für Biochemie, Martinsried, FRG.
authors.forename: M
authors.initials: M
authors.lastname: Aumailley
authors.forename: M
authors.initials: M
authors.lastname: Gerl
authors.forename: A
authors.initials: A
authors.lastname: Sonnenberg
authors.forename: R
authors.initials: R
authors.lastname: Deutzmann
authors.forename: R
authors.initials: R
authors.lastname: Timpl
mesh_terms: D001665:Binding Sites; D002448:Cell Adhesion; D016023:Integrins / Q000378:metabolism; D007797:Laminin / Q000032:analysis*; D009842:Oligopeptides / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis*; D011487:Protein Conformation
chemical_list: D016023:Integrins; D007797:Laminin; D009842:Oligopeptides; D010446:Peptide Fragments; C047981:arginyl-glycyl-aspartic acid