Major prion protein
UniProt P04925 · gene Prnp · Mus musculus · 254 residues
52evidence items
0mapped to a state
0states
9techniques
7sources
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).
| State | Basis | xray | cryoem | microed | nmr_structure | nmr_shifts | saxs_sans | force_spectroscopy | af_prediction | md | Total |
|---|---|---|---|---|---|---|---|---|---|---|---|
| No states defined yet. | |||||||||||
Unmapped evidence: 52 of 52 items. Mappings come from curator assignments and curated rules; see About for how rules work.
Sources
| Source | Evidence | Mapped |
|---|---|---|
| AlphaFold DB | 1 | 0 |
| BMRB | 14 | 0 |
| DisProt | 1 | 0 |
| MDDB | 1 | 0 |
| RCSB PDB | 31 | 0 |
| SASBDB | 3 | 0 |
| SMASH-BIO | 1 | 0 |
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.
| State | Basis | Parent | Description |
|---|
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.
| Evidence | Technique | Observable | Conditions | Mapped to state |
|---|---|---|---|---|
| EV-PDB-1AG2-1 RCSB PDB | nmr_structure | structure | in vitro · 19.85 °C · pH 4.5 PRION PROTEIN DOMAIN PRP(121-231) FROM MOUSE, NMR, 2 MINIMIZED AVERAGE STRUCTURE · MAJOR PRION PROTEIN (chains A) | unmapped |
| EV-PDB-1XYX-1 RCSB PDB | nmr_structure | structure | in vitro · 19.85 °C · pH 4.5 mouse prion protein fragment 121-231 · Major prion protein (chains A) | unmapped |
| EV-PDB-1Y15-1 RCSB PDB | nmr_structure | structure | in vitro · 19.85 °C · pH 4.5 Mouse Prion Protein with mutation N174T · Major prion protein (chains A) | unmapped |
| EV-PDB-2KFM-1 RCSB PDB | nmr_structure | structure | in vitro · 19.95 °C · pH 4.5 Mouse Prion Protein (121-231) with Mutations Y225A and Y226A · Major prion protein (chains A) | unmapped |
| EV-PDB-2KFO-1 RCSB PDB | nmr_structure | structure | in vitro · 19.95 °C · pH 4.5 Mouse Prion Protein (121-231) with Mutation V166A · Major prion protein (chains A) | unmapped |
| EV-PDB-2KU5-1 RCSB PDB | nmr_structure | structure | in vitro · 24.85 °C · pH 10 Mouse Prion Protein (121-231) with mutation D167S · Major prion protein (chains A) | unmapped |
| EV-PDB-2KU6-1 RCSB PDB | nmr_structure | structure | in vitro · 24.85 °C · pH 10 Mouse Prion Protein (121-231) with mutations D167S and N173K · Major prion protein (chains A) | unmapped |
| EV-PDB-2L1D-1 RCSB PDB | nmr_structure | structure | in vitro · 20.05 °C · pH 4.5 Mouse prion protein (121-231) containing the substitution Y169G · Major prion protein (chains A) | unmapped |
| EV-PDB-2L1E-1 RCSB PDB | nmr_structure | structure | in vitro · 20.05 °C · pH 4.5 Mouse prion protein (121-231) containing the substitution F175A · Major prion protein (chains A) | unmapped |
| EV-PDB-2L1H-1 RCSB PDB | nmr_structure | structure | in vitro · 20.05 °C · pH 4.5 Mouse prion protein fragment 121-231 at 20 C · Major prion protein (chains A) | unmapped |
| EV-PDB-2L1K-1 RCSB PDB | nmr_structure | structure | in vitro · 20.05 °C · pH 4.5 Mouse prion protein (121-231) containing the substitutions Y169A, Y225A, and Y226A · Major prion protein (chains A) | unmapped |
| EV-PDB-2L39-1 RCSB PDB | nmr_structure | structure | in vitro · 37.05 °C · pH 4.5 Mouse prion protein fragment 121-231 AT 37 C · Major prion protein (chains A) | unmapped |
| EV-PDB-2L40-1 RCSB PDB | nmr_structure | structure | in vitro · 20.05 °C · pH 4.5 Mouse prion protein (121-231) containing the substitution Y169A · Major prion protein (chains A) | unmapped |
| EV-PDB-3NVH-1 RCSB PDB | xray | resolution: 1.61 Å | in vitro · -173.15 °C · pH 7 · ligands TFA MIHFGND segment 137-143 from mouse prion · Major prion protein (chains A) | unmapped |
| EV-PDB-4H88-1 RCSB PDB | xray | resolution: 1.9 Å | in vitro · -173.15 °C · pH 6.5 · ligands NA Structure of POM1 FAB fragment complexed with mouse PrPc Fragment 120-230 · Major prion protein (chains A) | unmapped |
| EV-PDB-4J8R-3 RCSB PDB | xray | resolution: 2.303 Å | in vitro · -173.15 °C · pH 7.5 Structure of an octapeptide repeat of the prion protein bound to the POM2 Fab antibody fragment · Major prion protein (chains I,J) | unmapped |
| EV-PDB-4MA7-1 RCSB PDB | xray | resolution: 1.97 Å | in vitro · -173.15 °C · pH 6.5 · ligands P2Z Crystal structure of mouse prion protein complexed with Promazine · Major prion protein (chains A) | unmapped |
| EV-PDB-4MA8-1 RCSB PDB | xray | resolution: 2.2 Å | in vitro · -173.15 °C · pH 6.5 · ligands Z80 Crystal structure of mouse prion protein complexed with Chlorpromazine · Major prion protein (chains C) | unmapped |
| EV-PDB-6AQ7-1 RCSB PDB | xray | resolution: 1.83 Å | in vitro · -173.15 °C · pH 7 · ligands GOL, TCE Structure of POM6 FAB fragment complexed with mouse PrPc · Major prion protein (chains A) | unmapped |
| EV-PDB-6HER-1 RCSB PDB | xray | resolution: 1.199 Å | in vitro · -173.15 °C · pH 8 · ligands GOL, SO4 Mouse prion protein in complex with Nanobody 484 · Major prion protein (chains A) | unmapped |
| EV-PDB-6HHD-1 RCSB PDB | xray | resolution: 2.102 Å | in vitro · -173.15 °C · pH 6 · ligands CL, GOL, NA, SO4 Mouse Prion Protein in complex with Nanobody 484 · Major prion protein (chains A) | unmapped |
| EV-PDB-6HHD-3 RCSB PDB | xray | resolution: 2.102 Å | in vitro · -173.15 °C · pH 6 · ligands CL, GOL, NA, SO4 Mouse Prion Protein in complex with Nanobody 484 · Major prion protein (chains C) | unmapped |
| EV-PDB-7QIG-1 RCSB PDB | cryoem | resolution: 2.7 Å | in vitro Infectious mouse-adapted RML scrapie prion fibril purified from terminally-infected mouse brains · Major prion protein (chains A,B,C) | unmapped |
| EV-PDB-7TD6-1 RCSB PDB | cryoem | resolution: 3 Å | in vitro aRML prion fibril · Major prion protein (chains 1,A,B,C,D) | unmapped |
| EV-PDB-8A00-1 RCSB PDB | cryoem | resolution: 2.6 Å | in vitro Infectious mouse-adapted ME7 scrapie prion fibril purified from terminally-infected mouse brains · Major prion protein (chains A,B,C) | unmapped |
| EV-PDB-8DJA-1 RCSB PDB | cryoem | resolution: 3.92 Å | in vitro Cryo-EM structure of mouse PrP23-144 amyloid fibrils (polymorph 1) · Major prion protein (chains A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T) | unmapped |
| EV-PDB-8EFU-1 RCSB PDB | cryoem | resolution: 3.2 Å | in vitro a22L prion fibril · Major prion protein (chains A,B,C,D,E) | unmapped |
| EV-PDB-7RVD-1 RCSB PDB | microed | resolution: 1.003 Å | in vitro · -173.15 °C · pH 6 Segment from the mouse/cow prion protein 168-176 QYSNQNNFV · Major prion protein (chains A) | unmapped |
| EV-PDB-3NVG-1 RCSB PDB | xray | resolution: 1.48 Å | in vitro · -173.15 °C · pH 7.5 MIHFGN segment 137-142 from mouse prion · Major prion protein (chains A) | unmapped |
| EV-PDB-2K5O-1 RCSB PDB | nmr_structure | structure | in vitro · 25.05 °C · pH 4.5 Mouse Prion Protein (121-231) with Mutation S170N · Major prion protein (chains A) | unmapped |
| EV-PDB-1Y16-1 RCSB PDB | nmr_structure | structure | in vitro · 19.85 °C · pH 4.5 mouse prion protein with mutations S170N and N174T · Major prion protein (chains A) | unmapped |
| EV-BMRB-15053 BMRB | nmr_shifts | chemical_shift | in vitro · 26.85 °C · pH 5 HPRP-173-195 SOLUTION STRUCTURE · BMRB data: 1H chemical shifts | unmapped |
| EV-BMRB-15054 BMRB | nmr_shifts | chemical_shift | in vitro · 26.85 °C · pH 5 HPRP180-195 STRUCTURE · BMRB data: 1H chemical shifts | unmapped |
| EV-BMRB-15845 BMRB | nmr_shifts | chemical_shift | in vitro · 25.05 °C · pH 4.5 Mouse Prion Protein (121-231) with Mutation S170N · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-16184 BMRB | nmr_shifts | chemical_shift | in vitro · 19.95 °C · pH 4.5 Mouse Prion Protein (121-231) with Mutations Y225A and Y226A · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-16185 BMRB | nmr_shifts | chemical_shift | in vitro · 19.95 °C · pH 4.5 Mouse Prion Protein (121-231) with Mutation V166A · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-16722 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 4.5 mPrP_D167S · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-16723 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 4.5 mPrP_D1567D_N173K · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-17081 BMRB | nmr_shifts | chemical_shift | in vitro · 20.05 °C · pH 4.5 Mouse Prion Protein (121-231) with mutation Y169G · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-17082 BMRB | nmr_shifts | chemical_shift | in vitro · 20.05 °C · pH 4.5 Mouse Prion Protein (121-231) with mutation F175A · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-17084 BMRB | nmr_shifts | chemical_shift | in vitro · 20.05 °C · pH 4.5 NMR structure of mouse PrP fragment 121-231 at 20 C. · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-17174 BMRB | nmr_shifts | chemical_shift | in vitro · 37.05 °C · pH 4.5 MOUSE PRION PROTEIN FRAGMENT 121-231 AT 37 C · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-17213 BMRB | nmr_shifts | chemical_shift | in vitro · 20.05 °C · pH 4.5 Mouse prion protein (121-231) with the mutation Y169A · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-17758 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 2 Backbone 1H and 13C Chemical Shift Assignments of murine prion protein (residues 121-232) in its oxidized state · BMRB data: 13C chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-5197 BMRB | nmr_shifts | chemical_shift | in vitro · 19.85 °C · pH 4.5 1H and 13CA chemical shift assignments of the polypeptide mPrP(143-158) · BMRB data: 1H chemical shifts, 13C chemical shifts | unmapped |
| EV-SASBDB-SASDCJ2 SASBDB | saxs_sans | radius_of_gyration: 3.92 nm ± 0.02 | in vitro · 9.8 °C · pH 5.1 · ligands partner: P-Clone Fab, Chimera Prion Protein-Antibody Complexes Characterized by Chromatography-Coupled Small-Angle X-Ray Scattering. · Major prion protein with P-Clone Fab, Chimera | unmapped |
| EV-SASBDB-SASDHV9 SASBDB | saxs_sans | radius_of_gyration: 2.78 nm ± 0.04 | in vitro · 20 °C · pH 7.5 Characterization of murine prion protein · Major prion protein | unmapped |
| EV-SASBDB-SASDLU2 SASBDB | saxs_sans | radius_of_gyration: 8.13 nm ± 0.2 | in vitro · 20 °C · pH 7.4 · ligands partner: Anti-prion protein monoclonal IgG2a 6D11 Ligands binding to the prion protein induce its proteolytic release with therapeutic potential in neurodegenerative proteinopathies. · Major prion protein with Anti-prion protein monoclonal IgG2a 6D11 | unmapped |
| EV-DISPROT-DP00265r005 DisProt | nmr_shifts | disorder_region: 98 residues | in vitro DisProt DP00265: disorder, residues 23-120 · residues 23-120; evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion | unmapped |
| EV-AFDB-AF-P04925-F1 AlphaFold DB | af_prediction | plddt: 64.62 pLDDT | in silico AlphaFold DB prediction AF-P04925-F1 · AlphaFold Monomer v2.0 pipeline, residues 1-254 | unmapped |
| EV-MDDB-A003P MDDB | md | trajectory: 10 ns | in silico · 26.85 °C MoDEL 1AG2 · start 1AG2; Amber Parm99 | unmapped |
| EV-SMASH-SMFS-001503 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 8 Evidence of Orientation-Dependent Early States of Prion Protein Misfolded Structures from Single Molecule Force Spectroscopy. · Prion protein; afm smfs; experiment class: unfolding_protein | unmapped |
Conflicts
No conflicts found among comparable evidence.
49 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.