This analysis indicated that residue 37 was a major determinant of the electrostatic properties of pocket P9 of the peptide-binding groove.
Taken together, our findings suggest that the association of residues 37 and 86 with PSC primarily reflects the properties of pocket P9.
Investigations into the HLA-DR molecular structure revealed that the electrostatic properties of pocket P9 are determined by residue 37 and, indirectly by residue 86, suggesting that the P9 pocket is crucial for PSC risk.
Conclusion: The results suggest that in patients with PSC, residues 37 and 86 of the HLA-DRβ chain critically influence the electrostatic properties of pocket P9 and thereby the range of peptides presented.
In the HLA-DR molecule, residue 37 of the β chain appeared to be a key determinant of the electrostatic properties of pocket P9, which may be related to disease risk.
33, 34 A more remarkable difference between HLA-DRB1*13:01 and DRB1*13:02 encoded HLA-DR molecules was that the amino acid substitution at residue 86 affected the electrostatic properties of pocket P9, in another part of the molecule.
This study investigated properties of soil pockets of isolated arid mountains (i.e. inselbergs), asking the following questions:.
This implies that the physicochemical properties of the pockets at the interfaces of these PPIs are similar to each other.
For small molecules, only the binding pockets are considered as potential binding sites and a prediction is made for each pocket as to whether or not it binds a particular ligand, based on the properties of the pocket.
Consistent with the statistical observations, variation at residue 86 also indirectly influenced the electrostatic properties of this pocket.
The following properties of each pocket were used for the prediction of small molecule binding sites: nearby residue pair counts, residue propensity log P-values, evolutionary conservation log P-value, pocket volume and pocket principal components.
