Amyloid-beta precursor protein

UniProt P12023 · gene App · Mus musculus · 770 residues

16evidence items
0mapped to a state
0states
6techniques
4sources
0conflicts

Coverage grid

Mapped evidence per state and technique. Shaded rows rest on a single technique. Badge = best data level in the cell: raw (traces, images, FIDs: can be re-analysed), proc (maps, curves, tables, trajectories) or rep (values in the paper only).

StateBasisxraycryoemnmr_structurenmr_shiftsforce_spectroscopyaf_predictionTotal
No states defined yet.

Unmapped evidence: 16 of 16 items. Mappings come from curator assignments and curated rules; see About for how rules work.

Sources

SourceEvidenceMapped
AlphaFold DB10
BMRB80
RCSB PDB60
SMASH-BIO10

Structure

No state models are exported for this protein yet. Observed states export the representative PDB entry; inferred states need fitted models, not yet built.

States and transitions

No states defined.

StateBasisParentDescription

No transitions recorded in this version (no rate or free-energy evidence has been curated yet).

Evidence

One row per deposit or experiment. Filter by technique, environment or text. Unmapped evidence is listed too.

EvidenceTechniqueObservableConditionsMapped to state
EV-PDB-4YN0-2
RCSB PDB
xrayresolution: 2.2 Åin vitro · -173.15 °C · pH 8.6 · ligands MG, NAG
Crystal structure of APP E2 domain in complex with DR6 CRD domain · Amyloid beta A4 protein (chains B)
unmapped
EV-PDB-5MYK-3
RCSB PDB
xrayresolution: 1.6 Åin vitro · -173.15 °C · pH 7.5
Structure of Pyroglutamate-Abeta-specific Fab c#17 in complex with murine Abeta-pE3-18PEGb · Amyloid beta A4 protein (chains C)
unmapped
EV-PDB-7MRN-2
RCSB PDB
xrayresolution: 3.5 Åin vitro · -173.15 °C
Mouse CNTN5 APP complex · N-APP (chains C,D)
unmapped
EV-PDB-8S4Y-1
RCSB PDB
xrayresolution: 2.7 Åin vitro · -173.15 °C · pH 8.5
Crystal structure of an APP-talin (F2F3) chimera · C31 (chains A)
unmapped
EV-PDB-8BG9-1
RCSB PDB
cryoemresolution: 3.5 Åin vitro
Murine amyloid-beta filaments with the Arctic mutation (E22G) from APP(NL-G-F) mouse brains | ABeta · Amyloid-beta protein 40 (chains A,B)
unmapped
EV-PDB-2ROZ-1
RCSB PDB
nmr_structurestructurein vitro · 22.85 °C · pH 7
Structure of the C-terminal PID Domain of Fe65L1 Complexed with the Cytoplasmic Tail of APP Reveals a Novel Peptide Binding Mode · peptide from Amyloid beta A4 protein (chains A)
unmapped
EV-BMRB-10236
BMRB
nmr_shiftschemical_shiftin vitro · 22.85 °C · pH 7
Structure of the C-terminal PID Domain of Fe65L1 Complexed with the Cytoplasmic Tail of APP Reveals a Novel Peptide Binding Mode · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts
unmapped
EV-BMRB-15775
BMRB
nmr_shiftschemical_shiftin vitro · 44.85 °C · pH 6.5
Backbone chemical shift assignment for the transmembrane and C-terminal domains of amyloid precursor protein (APP C99) · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts
unmapped
EV-BMRB-17884
BMRB
nmr_shiftschemical_shiftin vitro · 4.85 °C · pH 7.1
METAL BINDING DOMAIN OF RAT BETA-AMYLOID · BMRB data: 13C chemical shifts, 1H chemical shifts
unmapped
EV-BMRB-18080
BMRB
nmr_shiftschemical_shiftin vitro · -0.15 °C · pH 4.6
structure of amyloid precursor protein's transmembrane domain · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts
unmapped
EV-BMRB-18649
BMRB
nmr_shiftschemical_shiftin vitro · 39.85 °C · pH 7.2
Transmembrane domain of Amyloid precursor protein WT · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts
unmapped
EV-BMRB-19701
BMRB
nmr_shiftschemical_shiftin vitro · 4.85 °C · pH 7
NMR structure of the soluble A 17-34 peptide · BMRB data: 1H chemical shifts
unmapped
EV-BMRB-5735
BMRB
nmr_shiftschemical_shiftin vitro · 24.85 °C
The Solution Structure of Rat Ab-(1-28) and its Interaction with Zinc: Insights into the Scarity of Amyloid Deposition in Aged Rat Brain · BMRB data: 1H chemical shifts
unmapped
EV-BMRB-6236
BMRB
nmr_shiftschemical_shiftin vitro · 26.85 °C · pH 6.4
Backbone 1H, 13C, and 15N Chemical Shift Assignments for CAPPD*, an Independently Folded Extracellular Domain of Human Amyloid-beta Precursor Protein · BMRB data: 1H chemical shifts, 13C chemical shifts, 15N chemical shifts
unmapped
EV-AFDB-AF-P12023-F1
AlphaFold DB
af_predictionplddt: 67.06 pLDDTin silico
AlphaFold DB prediction AF-P12023-F1 · AlphaFold Monomer v2.0 pipeline, residues 1-770
unmapped
EV-SMASH-SMFS-002089
SMASH-BIO
force_spectroscopystudy_recordin vitro
Pseudopeptide Amyloid Aggregation Inhibitors: In Silico, Single Molecule and Cell Viability Studies. · Amyloid-β; afm smfs; experiment class: unfolding_protein
unmapped

Conflicts

No conflicts found among comparable evidence.

16 evidence items could not be compared: they lack a comparable observable type, a value, or an uncertainty. Absence of a conflict here is not agreement.

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