EPM2A encodes for laforin, a dual-specificity protein phosphatase with a functional carbohydrate-binding domain (Ganesh et al, 2000), while EPM2B encodes for malin, an E3 ubiquitin ligase (Gentry et al, 2005).
A single functional cluster, carbohydrate derivative metabolic process, yielded the best CA score of 0.99, which includes complement C3 (CO3/C3, Uniprot/gene symbol), prothrombin (THRB/F2), vitamin D-binding protein (VTDB/GC), and v-type proton ATPase 16 kDa proteolipid subunit (VATL/Atp6v0c).
EPM2A encodes laforin, a dual specificity phosphatase of 331 amino acids with a functional carbohydrate binding domain at the N-terminus ([7], [8]).
These multiligand compounds often possess an additive or cooperative affinity toward multiple binding sites which is significantly higher than that of a single functional group interacting with a single binding site.
In this new system, each family contains members from a single carbohydrate binding-related domain.
Each galectin has an individual carbohydrate-binding preference.
It can function as a lectin, a carbohydrate-binding protein, which inhibits cellular activity.
SSIII-a and SSIII-b have a redundant carbohydrate-binding domain at the N terminus.
Such enzymes may contain single or multiple catalytic modules (GH) together with single or multiple noncatalytic carbohydrate-binding modules (CBMs) [ 10].
The present study also shows that some of the biological activities of M6P/IGF2R in SCC-VII cells strongly depend on a functional M6P-binding site within domain 3, thus providing further evidence for the non-redundant cellular functions of the individual carbohydrate-binding domains of the receptor.
