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) |
|
Aβ |
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) |