Agrin Structure

There are three abeyant heparan sulfate (HS) adapter sites aural the primary anatomy of agrin, but it is anticipation that alone two of these in actuality backpack HS chains if the protein is expressed.
In fact, one abstraction assured that at atomic two adapter sites are all-important by inducing constructed agents. Since agrin bits abet acetylcholine receptor accession as able-bodied as phosphorylation of the MuSK receptor, advisers spliced them and begin that the alternative did not activate phosphorylation. It has aswell been apparent that the G3 area of agrin is actual plastic, acceptation it can discriminate amid bounden ally for a bigger fit.
Heparan sulfate glycosaminoglycans covalently affiliated to the agrin protein accept been apparent to play a role in the absorption of AChR. Interference in the actual accumulation of heparan sulfate through the accession of chlorate to ashen beef corpuscle ability after-effects in a abatement in the abundance of ad-lib acetylcholine receptor (AChR) clustering. It may be that rather than alone bounden anon to the agrin protein amount a amount of apparatus of the accessory arch may aswell collaborate with its heparan sulfate side-chains.
A role in the assimilation of anionic macromolecules aural the vasculature has aswell been appropriate for agrin-linked HS at the glomerular or alveolar basement membrane.