In fact, different replacements of amino acids in the binding interfaces of both GI and GII NoVs are often seen, which serve as examples of some amino acids are replaceable in functional HBGA binding interfaces.
As shown by these studies, the binding interfaces of both strains are located in the same region of the outermost P2 domain, but the positions and amino acid composition of individual binding sites and the HBGA binding modes are different.
The HBGA-binding interface of Norwalk virus is located within a single monomer of the P dimer (Fig. 1, left panel), while the binding interface of VA387 involves both monomers of the P dimer (Fig. 1, right panel), although in both cases dimerization of the P domains appears to be required for their binding function [13], [14], [35].
On the other hand, the binding interface of the GII viruses (VA387) is composed of residues from both P1 and P2 subdomains and is located right at the interface of two monomers in the VA387 P dimer [13], [14], [15], [35].
Futran AS, Kyin S, Shvartsman SY, Link AJ: Mapping the binding interface of ERK and transcriptional repressor Capicua using photocrosslinking.
Grizot, S., Duclert, A., Thomas, S., Duchateau, P. & Paques, F. Context dependence between subdomains in the DNA binding interface of the I-CreI homing endonuclease.
Futran AS, Kyin S, Shvartsman SY, A Link J. Mapping the binding interface of ERK and transcriptional repressor Capicua using photocrosslinking.
The binding interface of calmodulin and a calmodulin binding peptide were reengineered by computationally designing complementary bumps and holes.
The binding interface of IL-8 and chondroitin sulfate determined this way correlated excellently with the corresponding NMR based atomistic model previously published.
The OsRac1 binding interface of RbohB is located in the flanking region of the coiled-coil region at N terminus.
