Type of interaction Protein complex Findings Ref.
Antibody-antigen Fab-GP41 MPER Induction of conformational changes in both the MPER and paratope during the process of core epitope recognition (Kim et al., 2011)
IgG1-FcRn Potential FcRn-binding interfaces in the Fab region (Jensen et al., 2015)
IgG4-TL1A A discontinuous epitope within the predicted interaction interface of TL1A and DR3 (Huang et al., 2018)
Fab-VEGF The identified epitope overlapping with the binding interface of the biological receptor of VEGF (Comamala et al., 2020)
IgG-CD20 peptide CDR3 (VH) functioning as the dominant antigen docking motif (Uhrik et al., 2021)
Fab-IL23 Peptide-level epitopes identified (Li et al., 2017)
Camelid single domain antibody-IL6/gp80 complex The junctional epitope present only in the IL6/gp80 complex, not in the individual components (Adams et al., 2017)
IgG-fHbp Four immunogenic regions located on the N- and C-termini of fHbp (Ständer et al., 2021)
IgG-transglutaminase 2 Main epitopes targeted by celiac disease autoantibodies (Iversen et al., 2014)
IgG-rAna o 2 Conformational and linear epitopes recognized respectively by two different antibodies (Zhang et al., 2011)
IgG-ANXA1 Interaction region within domain III of ANXA1 in Ca2+-bound conformation (Gramlich et al., 2021)
Antibody-Zika envelop Three spatially distinct epitopes for the six mAbs (Adhikari et al., 2021)
Fab- cytochrome c The epitope being in good agreement with the contact residues identified by the X-ray crystallographic structure (Coales et al., 2009)
IgG- rAna o 2 Five discontinuous, conformational epitopes (Guan et al., 2015)
IgG- rAna o 2 Four regions identified as potential epitopes (Zhang et al., 2013)
IgG1 self-association Major protein-protein interfaces associated with the concentration-dependent self-oligomerization of IgG (Arora et al., 2015)
Self-oligomer Apolipoprotein E Oligomerization via the C-terminal regions (Huang et al., 2011)
Tau Hyperphosphorylation-induced interface formation in the microtubule binding repeat region (Zhu et al., 2015)
β-2-Microglobulin The region spanned by Arg45-Leu54 serving as the interface for the dimer (Borotto et al., 2017)
α-synuclein The C-terminus acting as a fold (Stephens et al., 2018)
Sequence-specific engagement of side-chains of residues located at the N-terminal part in a network of oligomer-stabilizing interactions. (Przygońska et al., 2018)
Protein-lipid PTEN The membrane-binding helix in the N-terminal of PTEN (Masson et al., 2016)
β2AR The transmembrane domains embedded in bicellar region (Duc et al., 2015)
Homologous transporters: XylE, LacY and GlpT
Conserved networks of charged residues regulated by interactions with surrounding phospholipids, acting as molecular switches for the conformational transition
(Martens et al., 2018)
PTEN The salt bridge interactions between the basic residues and the lipids as a major driving force in stabilizing the protein-membrane interface (Jang et al., 2021)
Sphingosine kinase 1 A positively charged motif responsible for electrostatic interactions with membranes (Pulkoski-Gross et al., 2018)