IndraLab

Statements

sparser
"Structural Modelling of Interactions Between OTUD1 Peptide and FP."
41599331
sparser
"Hydrogen-bond occupancy analysis further supported that a subset of these contacts involved stable hydrogen bonds ( xref ), suggesting that the OTUD1–FP association predicted by AlphaFold3 is dynamically stable under explicit-solvent MD conditions."
41599331
sparser
"LIGPLOT [ xref ] analyses identified the key interacting residues that were constant across both these models, namely, that FP Leu 6 and Leu 7 interacted hydrophobically with OTUD1 residues 12 to 18, FP Leu 34 had hydrophobic interaction with OTUD1 Leu8 and His11, and a salt bridge between FP Asp33 and OTUD1 Arg12 ( xref )."
41599331
sparser
"These results demonstrate that the OTUD1–FP complex initially predicted by AlphaFold3 appears both structurally and energetically stable under physiological conditions, with the third alpha helix of the FP showing two alternative orientations."
41599331
sparser
"While it is possible that the OTUD1 peptide interaction with FP is mimicking the interaction of OTUD1 protein and FP during viral infection, it is also possible that the OTUD1 peptide may be mimicking some other natural ligand of FP."
41599331
sparser
"Our Alphafold3 prediction of FP and OTUD1 peptide interaction indicated that the OTUD1 peptide bound a similar wedge-like conformation of FP in a stable interaction, with positively charged residues on one face of the OTUD1 peptide’s alpha helix making stable contacts with some hydrophobic residues in FP."
41599331