Protegrin-5
UniProt P49934 · gene NPG5 · Sus scrofa · 149 residues
26evidence items
0mapped to a state
0states
4techniques
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).
| State | Basis | nmr_structure | nmr_shifts | force_spectroscopy | af_prediction | Total |
|---|---|---|---|---|---|---|
| No states defined yet. | ||||||
Unmapped evidence: 26 of 26 items. Mappings come from curator assignments and curated rules; see About for how rules work.
Sources
| Source | Evidence | Mapped |
|---|---|---|
| AlphaFold DB | 1 | 0 |
| BMRB | 2 | 0 |
| RCSB PDB | 1 | 0 |
| SMASH-BIO | 22 | 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-2NC7-1 RCSB PDB | nmr_structure | structure | in vitro · 19.85 °C Antimicrobial peptide protegrin PG-5 · Protegrin-5 (chains A) | unmapped |
| EV-BMRB-26009 BMRB | nmr_shifts | chemical_shift | in vitro · 19.85 °C Antimicrobial peptide protegrin PG-5 · BMRB data: 1H chemical shifts | unmapped |
| EV-BMRB-5688 BMRB | nmr_shifts | chemical_shift | in vitro · 26.85 °C · pH 6.2 Backbone 1H, 13C, and 15N Chemical Shifts Assignment for the all-trans conformer of the cathelin-like domain of the protegrin-3 precursor · BMRB data: 1H chemical shifts, 13C chemical shifts, 15N chemical shifts | unmapped |
| EV-AFDB-AF-P49934-F1 AlphaFold DB | af_prediction | plddt: 81.12 pLDDT | in silico AlphaFold DB prediction AF-P49934-F1 · AlphaFold Monomer v2.0 pipeline, residues 1-149 | unmapped |
| EV-SMASH-SMFS-000293 SMASH-BIO | force_spectroscopy | study_record | in vitro Single-molecule force spectroscopy reveals a high-force requirement for dissociation of integrin transmembrane domains. · Integrins; optical tweezers; experiment class: receptor_ligand_adhesion, rheology_cell | unmapped |
| EV-SMASH-SMFS-000491 SMASH-BIO | force_spectroscopy | study_record | in cell Locked Nucleic Acid-Modified Force Probe Reveals High-Force Regulation of Yes-Associated Protein through Talin-Vinculin in Breast Cancer. · Integrins; tension sensors; experiment class: force_generation_motor, receptor_ligand_adhesion, rheology_cell | unmapped |
| EV-SMASH-SMFS-000696 SMASH-BIO | force_spectroscopy | study_record | in vitro Can a bulky glycocalyx promote catch bonding in early integrin adhesion? Perhaps a bit. · Integrins; force spectroscopy unspecified; experiment class: receptor_ligand_adhesion, rheology_cell | unmapped |
| EV-SMASH-SMFS-001068 SMASH-BIO | force_spectroscopy | study_record | in vitro Can a bulky glycocalyx promote catch bonding in early integrin adhesion? Perhaps a bit · Integrins; force spectroscopy unspecified; experiment class: receptor_ligand_adhesion, rheology_cell | unmapped |
| EV-SMASH-SMFS-001069 SMASH-BIO | force_spectroscopy | study_record | in vitro Can a bulky glycocalyx promote catch bonding in early integrin adhesion? Perhaps a bit · Integrins; force spectroscopy unspecified; experiment class: receptor_ligand_adhesion, rheology_cell | unmapped |
| EV-SMASH-SMFS-001209 SMASH-BIO | force_spectroscopy | study_record | in vitro Kindlin stabilizes the talin·integrin bond under mechanical load by generating an ideal bond. · Integrins; optical tweezers; experiment class: force_generation_motor, receptor_ligand_adhesion, rheology_cell | unmapped |
| EV-SMASH-SMFS-001597 SMASH-BIO | force_spectroscopy | study_record | in vitro Mechano-Redox Control of Integrins in Thromboinflammation. · Integrins; force spectroscopy unspecified; experiment class: receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-001712 SMASH-BIO | force_spectroscopy | study_record | in cell Single-Molecule Force Imaging Reveals That Podosome Formation Requires No Extracellular Integrin-Ligand Tensions or Interactions. · Integrins; tension sensors; experiment class: force_generation_motor, force_generation_polymerization, receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-001713 SMASH-BIO | force_spectroscopy | study_record | in vitro Single-Molecule Force Probing of RGD-Binding Integrins on Pancreatic Cancer Cells. · Integrins; afm smfs; experiment class: receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-001918-r0 SMASH-BIO | force_spectroscopy | rupture_force: 17.85 pN ± 0.63 | in vitro Examining the Effect of Kindlin-3 Binding Site Mutation on LFA-1-ICAM-1 Bonds by Force Measuring Optical Tweezers. · Integrins; optical tweezers; experiment class: receptor_ligand_adhesion, rheology_cell | unmapped |
| EV-SMASH-SMFS-001918-r1 SMASH-BIO | force_spectroscopy | loading_rate: 30.21 pN/s ± 4.35 | in vitro Examining the Effect of Kindlin-3 Binding Site Mutation on LFA-1-ICAM-1 Bonds by Force Measuring Optical Tweezers. · Integrins; optical tweezers; experiment class: receptor_ligand_adhesion, rheology_cell | unmapped |
| EV-SMASH-SMFS-001918-r2 SMASH-BIO | force_spectroscopy | rupture_force: 10.08 pN ± 0.88 | in vitro Examining the Effect of Kindlin-3 Binding Site Mutation on LFA-1-ICAM-1 Bonds by Force Measuring Optical Tweezers. · Integrins; optical tweezers; experiment class: receptor_ligand_adhesion, rheology_cell | unmapped |
| EV-SMASH-SMFS-002225 SMASH-BIO | force_spectroscopy | study_record | in vitro AFM Force Spectroscopy Reveals the Role of Integrins and Their Activation in Cell-Biomaterial Interactions. · Integrins; afm smfs; experiment class: receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-002495 SMASH-BIO | force_spectroscopy | study_record | in vitro Probing the recognition specificity of αVβ1 integrin and syndecan-4 using force spectroscopy. · Integrins; afm smfs; experiment class: receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-002764 SMASH-BIO | force_spectroscopy | study_record | in vitro Kindlin Is Mechanosensitive: Force-Induced Conformational Switch Mediates Cross-Talk among Integrins. · Integrins; force spectroscopy unspecified; experiment class: receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-003183 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7.4 Mechano-redox control of integrin de-adhesion. · Integrins; force spectroscopy unspecified; experiment class: receptor_ligand_adhesion, rheology_cell | unmapped |
| EV-SMASH-SMFS-003516 SMASH-BIO | force_spectroscopy | study_record | in vitro Force regulated conformational change of integrin αVβ3. · Integrins; biomembrane force probe; experiment class: receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-003933 SMASH-BIO | force_spectroscopy | study_record | in cell · pH 7.6 Integrins outside focal adhesions transmit tensions during stable cell adhesion. · Integrins; tension sensors; experiment class: force_generation_motor, receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-005118 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7.4 Bimolecular integrin-ligand interactions quantified using peptide-functionalized dextran-coated microparticles. · Integrins; optical tweezers; experiment class: receptor_ligand_adhesion, rheology_cell | unmapped |
| EV-SMASH-SMFS-005587 SMASH-BIO | force_spectroscopy | study_record | in vitro Negative feedback from integrins to cadherins: a micromechanical study. · Integrins; optical tweezers; experiment class: receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-006885 SMASH-BIO | force_spectroscopy | study_record | in vitro Rigidity sensing at the leading edge through alphavbeta3 integrins and RPTPalpha. · Integrins; optical tweezers; experiment class: receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-007689 SMASH-BIO | force_spectroscopy | study_record | in vitro Integrin-cytoskeletal interactions in migrating fibroblasts are dynamic, asymmetric, and regulated. · Integrins; optical tweezers; experiment class: receptor_ligand_adhesion, rheology_cell, translation_transcription_replication | unmapped |
Conflicts
No conflicts found among comparable evidence.
26 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.