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. 2016 Jun 23;291(34):17727–17742. doi: 10.1074/jbc.M116.735258

TABLE 1.

Asn347 glycosylation, in particular the triantennary glycoforms, causes more perturbation of the average RCL conformation relative to the non-glycosylated RCL structure

Perturbation, which may restrict access of or affect recognition by the RCL-targeting proteases, was measured as the average root mean square deviation (Å) (mean ± S.D.) of the Cα atoms of the RCL over the course of the simulations (t = 100 ns, n = 1,000 sampled time points) of the Asn347 glycoforms of CBG relative to the average structure adopted by the RCL Cα atoms in the non-glycosylated CBG variant.

CBG Asn347 glycoform Perturbation of the RCL conformation (RMSD) (mean ± S.D.)
Å
Non-glycosylated 1.5 ± 0.4a
BS2 2.4 ± 0.3
TS3-A 4.1 ± 0.5
TS3-B 3.1 ± 0.4
TS3f-A 3.1 ± 0.4
TS3f-B 3.5 ± 0.7
DTS3-A 3.9 ± 0.4
DTS3-B 3.5 ± 0.6

a This value represents the baseline deviation from the average RCL structure without perturbation by an attached glycan. See the legend to Fig. 1 and supplemental Table S1 for the Asn347 glycoform nomenclature used here.