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Importantly, direct binding of the LES TCR to EPCR was confirmed by surface plasmon resonance, showing relatively low binding affinity (KD ≈ 90 µM) (Table 3).
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PpGalec was implicated in the specific binding of the Le.
The loss or degeneration of the H epitope/acetamido binding site and the reinforcement of the Le binding site of the GI.8 BV is a typical example of such change selected by the host Lewis epitope.
In GI.2 FUV the much longer P-loop reaches the HBGA binding interface and two residues (G343′ and G245′) are involved in the formation of the Le epitope binding site (Kubota et al., 2012).
(D) A close-up of the Le antigen binding interface with indication of each amino acid component.
Thus, both the length and sequence compositions of the P-loop are important in the formation of the Le epitope binding site.
Another piece of evidence in supporting this hypothesis is the participation of V442 of the S-loop in the formation of the Le epitope binding site.
Structural and sequence comparisons among the four GI P domains indicate that the P-loop provides the major components of the Le epitope binding site (Figs. 1, 5 and 6).
The two P monomers are shown in purple and cyan, respectively, while the P- and S-loops that are involved in the formation of the Le epitope binding site are in yellow and blue.
The β-1,3 Gal binding site is conserved with the other three GI NoVs, while the Le epitope binding sites are particularly well developed, formed by five residues and interact with Le epitope via six hydrogen (H) bonds, highlighting the importance of the Le epitope binding site in BV.
In addition, the two P-loops of a P dimer that are the major components of the Le epitope binding sites (see below) are closer to each other in GI.1 NV, occupying the central area of the top surface of the P dimer.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com