Formation of homodimers by identical Dscam1 protein isomers on cell surface is the key factor for the self-avoidance of growing neurites. Dscam1 immense diversity has a critical role in the formation of arthropod neuronal circuit, showing unique evolutionary properties when compared to other cell surface proteins. Experimental measures are available for 89 self-binding and 1722 hetero-binding protein samples, out of more than 19 thousands (self-binding) and 350 millions (hetero-binding) possible isomer combinations.Results:
We developed Dscam1 Web Server to quickly predict Dscam1 self- and hetero- binding affinity for batches of Dscam1 isomers. The server can help the study of Dscam1 affinity and help researchers navigate through the tens of millions of possible isomer combinations to isolate the strong-binding ones.Availability and Implementation:
Dscam1 Web Server is freely available at: http://bioinformatics.tecnoparco.org/Dscam1-webserver. Web server code is available at https://gitlab.com/ne1s0n/Dscam1-binding.Contact:
email@example.com or firstname.lastname@example.orgSupplementary information:
Supplementary data are available at Bioinformatics online.