The 380s Loop is proposed to be potentially a determinant of SS-specificity and through its involvement in the open-closed transition of the active site during ADPglucose binding as has been suggested for glycogen phosphorylases.
Through a pharmacophore approach, complementarities between the ligand and the binding site are explored and a plausible mode of binding with the protein is suggested for albidoside.
This would be in agreement with the apparent multiple binding components that have been suggested for polyamine-induced rectification of channels [50], [51], [52], [53].
It is possible that this Ub-binding ability could recruit a Ub-charged E1 in a Ub-dependent manner, as has been suggested for Ub binding domain (UBD -driven, E3-independent monoUBD -drivenion reactions (Hoeller et al, 2007).
By contrast, not more than nine FG-binding sites have so far been suggested for mammalian Impβ (Isgro & Schulten, 2005).
This mechanism has recently been suggested for the binding of the first two UIM regions from ataxin-3 to ubiquitin where it is suggested that the UIMs adopt a more compact structure upon binding.
A single function has been suggested for the lipid, binding to the membrane and thus elevating the local concentration of the peptide at the target site.
Therefore NanU must either improve the efficiency of this system in the gut and oral cavity, where both competition for sialic acid and its bioavailability might be reduced, or that NanU acts to store sialic acid on the surface of these bacteria as has been suggested for the starch-binding protein SusD [ 40].
One of these sites, HS1, was shown to be pro-B cell specific, the stage during which IgH V(D J recombination takes place, and was suggested to include binding sites for the transcription factors PU.1, Pax5 and E2A [9].
This loop was suggested to be a binding region for kinetin [ 39] and to play an essential role in IgG and IgE binding [ 6, 7, 43, 44], making it a general IgE binding epitope responsible for cross reactions between Bet v 1 homologous proteins [ 4].
