The tripeptide Arginine-Glycine-Aspartic acid (RGD) is usually conformed as a loop and it can be found in all life forms, from virus to human. In homologous proteins it may or may not be conserved, the latter usually showing a change or loss of functionality. Its main function lies with proteins implicated to cell adhesion; the loop formation, however, with the charged side chains of D and R looking outwards and away from each other, constitutes a drastic and very distinct 3-D entity. This combination allows a wide range of bond-centered interactions, as in signal transduction. The RGD is routinely-though not exclusively- found in transmembranic proteins, usually faced outwards. Its functions are regulated by neighboring amino acids, which may provide either agility or rigidity.
The dispersion and abundance of RGD throughout the biosphere and the variety of its functions impose the need for massive data compilation and comparison to elucidate its role and impact.
To represent information in a form enabling interested parties to digest the large amounts of information without losing perspective, the RGDtrip proteins data collection provides users with advanced interface technology to complete and further their research an intuitive way.See software requirements