Arginylglycylaspartic acid (RGD) is the most common peptide motif responsible for cell adhesion to the extracellular matrix (ECM), found in species ranging from Drosophila to humans.

The tripeptide Arg-Gly-Asp (RGD) was originally identified as the sequence within fibronectin that mediates cell attachment. The RGD motif has now been found in numerous other proteins and supports cell adhesion in many, but not all, of these.

2023年1月2日 · RGD-binding integrins refer to a class of integrins that bind with the tripeptide motif Arg–Gly–Asp in ECM proteins, including αvβ1, αvβ3, αvβ5, αvβ6, αvβ8, α5β1, α8β1, and ...

2024年2月4日 · The RGD motif is a short peptide sequence found in various ECM proteins, such as fibronectin, vitronectin, and collagen. It plays a crucial role in cell adhesion and migration by interacting with integrin receptors. The arginine residue in the RGD motif forms a salt bridge with a conserved glutamic acid residue in the integrin receptor, while ...

An interaction between Sema7A and β-integrins was predicted from the presence of an arginine-glycine-aspartate amino acid sequence, known as an RGD-motif, in the Sema7A sema domain. The RGD-motif is a recognition site for integrin receptors and is present in integrin ligands such as extracellular matrix (ECM) molecules.

2023年1月24日 · The arginine-glycine-aspartic acid (RGD) motif is a cell adhesion sequence that binds to integrins. Some RGD-contg. peptides promote adhesion of both embryonic stem cells and induced pluripotent stem cells (iPSCs); however, not all such RGD-contg. peptides are active.

Many adhesive proteins present in extracellular matrices and in the blood contain the tripeptide arginine-glycine-aspartic acid (RGD) as their cell recognition site. These proteins include fibronectin, vitronectin, osteopontin, collagens, thrombospondin, fibrinogen, and …