Tropomyosin alpha-1 chain

UniProt P09493 · gene TPM1 · Homo sapiens · 284 residues

42evidence 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: 42 of 42 items. Mappings come from curator assignments and curated rules; see About for how rules work.

Sources

SourceEvidenceMapped
AlphaFold DB10
BMRB30
RCSB PDB160
SMASH-BIO220

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-3MUD-2
RCSB PDB
xrayresolution: 2.2 Åin vitro · -173.15 °C · pH 6.5 · ligands EDO, SO4
Structure of the Tropomyosin Overlap Complex from Chicken Smooth Muscle · Tropomyosin alpha-1 chain,Microtubule-associated protein RP/EB family member 1 (chains C,D)
unmapped
EV-PDB-6KN8-3
RCSB PDB
cryoemresolution: 4.8 Åin vitro · ligands ADP
Structure of human cardiac thin filament in the calcium bound state · Tropomyosin alpha-1 chain (chains R,S,Y,Z)
unmapped
EV-PDB-6KN8-2
RCSB PDB
cryoemresolution: 4.8 Åin vitro · ligands ADP
Structure of human cardiac thin filament in the calcium bound state · Tropomyosin alpha-1 chain (chains P,Q,W,X)
unmapped
EV-PDB-6UT2-2
RCSB PDB
nmr_structurestructurein vitro · 24.85 °C · pH 6.5
3D structure of the leiomodin/tropomyosin binding interface · Tropomyosin alpha-1 chain chimeric peptide (chains B,C)
unmapped
EV-PDB-7UTI-2
RCSB PDB
cryoemresolution: 4.8 Åin vitro · ligands ADP, CA, MG
ALTERNATIVE MODELING OF TROPOMYOSIN IN HUMAN CARDIAC THIN FILAMENT IN THE CALCIUM BOUND STATE · Tropomyosin alpha-1 chain (chains W,b,e,f,g,h,i,j)
unmapped
EV-PDB-7UTL-2
RCSB PDB
cryoemresolution: 6.6 Åin vitro · ligands ADP, MG
ALTERNATIVE MODELING OF TROPOMYOSIN IN HUMAN CARDIAC THIN FILAMENT IN THE CALCIUM FREE STATE · Tropomyosin alpha-1 chain (chains W,Z,a,b,g,h,i,j)
unmapped
EV-PDB-8EFH-3
RCSB PDB
cryoemresolution: 3.3 Åin vitro · ligands ADP, MG
Helical reconstruction of the human cardiac actin-tropomyosin-myosin complex in complex with ADP-Mg2+ · Tropomyosin alpha-1 chain (chains O,P)
unmapped
EV-PDB-8EFI-3
RCSB PDB
cryoemresolution: 3.4 Åin vitro · ligands ADP, MG
Helical reconstruction of the human cardiac actin-tropomyosin-myosin complex in the rigor form · Tropomyosin alpha-1 chain (chains O,P)
unmapped
EV-PDB-8ENC-3
RCSB PDB
cryoemresolution: 3.6 Åin vitro · ligands ADP, MG
Helical reconstruction of the human cardiac actin-tropomyosin-myosin loop 4 7G mutant complex · Tropomyosin alpha-1 chain (chains O,P)
unmapped
EV-PDB-8ZB7-3
RCSB PDB
cryoemresolution: 3.19 Åin vitro · ligands ADP
Human left ventricle ATM complex · Tropomyosin alpha-1 chain (chains L,N,O,P)
unmapped
EV-PDB-9ZBL-2
RCSB PDB
cryoemresolution: 2.79 Åin vitro · ligands ADP, MG
Helical Reconstruction of the Human Cardiac F-Actin-Tropomyosin Complex · Tropomyosin alpha-1 chain (chains M,N,O,P)
unmapped
EV-PDB-9ZBP-2
RCSB PDB
cryoemresolution: 3.12 Åin vitro · ligands ADP, MG
Helical Reconstruction of the Complex of Pseudo-Acetylated Human Cardiac Actin (K326/328Q) and Tropomyosin · Tropomyosin alpha-1 chain (chains M,N,O,P)
unmapped
EV-PDB-6X5Z-2
RCSB PDB
cryoemresolution: 4.24 Åin vitro · ligands ADP, MG
Bovine Cardiac Myosin in Complex with Chicken Skeletal Actin and Human Cardiac Tropomyosin in the Rigor State · Tropomyosin alpha-1 chain (chains O,P)
unmapped
EV-PDB-6KN7-3
RCSB PDB
cryoemresolution: 6.6 Åin vitro · ligands ADP
Structure of human cardiac thin filament in the calcium free state · Tropomyosin alpha-1 chain (chains R,S,Y,Z)
unmapped
EV-PDB-6KN7-2
RCSB PDB
cryoemresolution: 6.6 Åin vitro · ligands ADP
Structure of human cardiac thin filament in the calcium free state · Tropomyosin alpha-1 chain (chains P,Q,W,X)
unmapped
EV-PDB-5KHT-1
RCSB PDB
xrayresolution: 1.4964 Åin vitro · -173.15 °C · pH 7.5 · ligands PEG
Crystal structure of the N-terminal fragment of tropomyosin isoform Tpm1.1 at 1.5 A resolution · Tropomyosin alpha-1 chain,General control protein GCN4 (chains A,B,C,D)
unmapped
EV-BMRB-30681
BMRB
nmr_shiftschemical_shiftin vitro · 24.85 °C · pH 6.5
3D structure of the leiomodin/tropomyosin binding interface · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts
unmapped
EV-BMRB-5610
BMRB
nmr_shiftschemical_shiftin vitro · -90.15 °C · pH 6.5
The Structure of the Carboxyl Terminus of Striated alpha-Tropomyosin in Solution Reveals an Unusual Parallel Arrangement of Interacting alpha-Helices · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts, coupling constants
unmapped
EV-BMRB-7080
BMRB
nmr_shiftschemical_shiftin vitro · 9.85 °C
Complex of TM1a(1-14)Zip with TM9a(251-284): a model for the polymerization domain ("overlap region")of tropomyosin · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts
unmapped
EV-AFDB-AF-P09493-F1
AlphaFold DB
af_predictionplddt: 91.62 pLDDTin silico
AlphaFold DB prediction AF-P09493-F1 · AlphaFold Monomer v2.0 pipeline, residues 1-284
unmapped
EV-SMASH-SMFS-000564
SMASH-BIO
force_spectroscopystudy_recordin vitro
Probing protein-protein interactions with drag flow: A case study of F-actin and tropomyosin · Troponin/tropomyosin regulatory complex; force spectroscopy unspecified; experiment class: force_generation_motor, rheology_cell
unmapped
EV-SMASH-SMFS-000565
SMASH-BIO
force_spectroscopystudy_recordin vitro
Probing protein-protein interactions with drag flow: a case study of F-actin and tropomyosin. · Troponin/tropomyosin regulatory complex; force spectroscopy unspecified; experiment class: force_generation_motor, rheology_cell
unmapped
EV-SMASH-SMFS-000784
SMASH-BIO
force_spectroscopystudy_recordin vitro · pH 7.3
Functional and Structural Properties of Cytoplasmic Tropomyosin Isoforms Tpm1.8 and Tpm1.9. · Troponin/tropomyosin regulatory complex; optical tweezers; experiment class: force_generation_motor, nucleic_acid_protein_interaction, receptor_ligand_adhesion, rheology_cell
unmapped
EV-SMASH-SMFS-001236
SMASH-BIO
force_spectroscopystudy_recordin vitro · pH 8
Micro-mechanical response and power-law exponents from the longitudinal fluctuations of F-actin solutions. · Troponin/tropomyosin regulatory complex; optical tweezers; experiment class: force_generation_motor, force_generation_polymerization, rheology_cell
unmapped
EV-SMASH-SMFS-001310
SMASH-BIO
force_spectroscopystudy_recordin vitro
Single Molecule Mechanics and Kinetics of Cardiac Myosin Interacting with Regulated Thin Filaments · Troponin/tropomyosin regulatory complex; force spectroscopy unspecified; experiment class: force_generation_motor
unmapped
EV-SMASH-SMFS-002655
SMASH-BIO
force_spectroscopystudy_recordin vitro
Cardiomyopathy-associated mutations in tropomyosin differently affect actin-myosin interaction at single-molecule and ensemble levels. · Troponin/tropomyosin regulatory complex; optical tweezers; experiment class: force_generation_motor
unmapped
EV-SMASH-SMFS-002737
SMASH-BIO
force_spectroscopystudy_recordin vitro
Functional significance of HCM mutants of tropomyosin, V95A and D175N, studied with in vitro motility assays. · Troponin/tropomyosin regulatory complex; optical tweezers; experiment class: force_generation_motor
unmapped
EV-SMASH-SMFS-003095
SMASH-BIO
force_spectroscopystudy_recordin vitro
Estimation of actomyosin active force maintained by tropomyosin and troponin complex under vertical forces in the in vitro motility assay system. · Troponin/tropomyosin regulatory complex; optical tweezers; experiment class: force_generation_motor, rheology_cell
unmapped
EV-SMASH-SMFS-003447
SMASH-BIO
force_spectroscopystudy_recordin vitro
Cooperativity of myosin interaction with thin filaments is enhanced by stabilizing substitutions in tropomyosin. · Troponin/tropomyosin regulatory complex; optical tweezers; experiment class: force_generation_motor
unmapped
EV-SMASH-SMFS-003868
SMASH-BIO
force_spectroscopystudy_recordin vitro · pH 7.4
Direct observation of the actin filament by tip-scan atomic force microscopy. · Troponin/tropomyosin regulatory complex; afm smfs; experiment class: force_generation_motor
unmapped
EV-SMASH-SMFS-003979
SMASH-BIO
force_spectroscopystudy_recordin vitro
Muscle Fatigue from the Perspective of a Single Crossbridge. · Troponin/tropomyosin regulatory complex; optical tweezers; experiment class: force_generation_motor
unmapped
EV-SMASH-SMFS-004382
SMASH-BIO
force_spectroscopystudy_recordin vitro
Stabilizing the central part of tropomyosin increases the bending stiffness of the thin filament. · Troponin/tropomyosin regulatory complex; optical tweezers; experiment class: force_generation_motor
unmapped
EV-SMASH-SMFS-004735
SMASH-BIO
force_spectroscopystudy_recordin vitro · pH 7.5
The role of caldesmon and its phosphorylation by ERK on the binding force of unphosphorylated myosin to actin. · Troponin/tropomyosin regulatory complex; optical tweezers; experiment class: force_generation_motor, receptor_ligand_adhesion
unmapped
EV-SMASH-SMFS-005309
SMASH-BIO
force_spectroscopystudy_recordin vitro
Recent insights into muscle fatigue at the cross-bridge level. · Troponin/tropomyosin regulatory complex; optical tweezers; experiment class: force_generation_motor
unmapped
EV-SMASH-SMFS-005310
SMASH-BIO
force_spectroscopystudy_recordin vitro
Recent insights into the molecular basis of muscular fatigue. · Troponin/tropomyosin regulatory complex; optical tweezers; experiment class: force_generation_motor
unmapped
EV-SMASH-SMFS-005509
SMASH-BIO
force_spectroscopystudy_recordin vitro
Force spectroscopy reveals multiple "closed states" of the muscle thin filament. · Troponin/tropomyosin regulatory complex; optical tweezers; experiment class: force_generation_motor, receptor_ligand_adhesion
unmapped
EV-SMASH-SMFS-005812
SMASH-BIO
force_spectroscopystudy_recordin vitro · pH 7.4
Human actin mutations associated with hypertrophic and dilated cardiomyopathies demonstrate distinct thin filament regulatory properties in vitro. · Troponin/tropomyosin regulatory complex; optical tweezers; experiment class: force_generation_motor
unmapped
EV-SMASH-SMFS-005993
SMASH-BIO
force_spectroscopystudy_recordin vitro
Antibody-antigen exchange equilibria in a field of an external force: design of reagentless biosensors. · Troponin/tropomyosin regulatory complex; magnetic tweezers; experiment class: receptor_ligand_adhesion
unmapped
EV-SMASH-SMFS-006143
SMASH-BIO
force_spectroscopystudy_recordin vitro · pH 7.4
Phosphorylation of tropomyosin extends cooperative binding of myosin beyond a single regulatory unit. · Troponin/tropomyosin regulatory complex; optical tweezers; experiment class: force_generation_motor
unmapped
EV-SMASH-SMFS-006915
SMASH-BIO
force_spectroscopystudy_recordin vitro
Temperature change does not affect force between regulated actin filaments and heavy meromyosin in single-molecule experiments. · Troponin/tropomyosin regulatory complex; optical tweezers; experiment class: force_generation_motor
unmapped
EV-SMASH-SMFS-007066-r0
SMASH-BIO
force_spectroscopystep_size: 5 nmin vitro
Single-myosin crossbridge interactions with actin filaments regulated by troponin-tropomyosin. · Troponin/tropomyosin regulatory complex; optical tweezers; experiment class: force_generation_motor
unmapped
EV-SMASH-SMFS-007668
SMASH-BIO
force_spectroscopystudy_recordin vitro
In vitro motility of immunoadsorbed brain myosin-V using a Limulus acrosomal process and optical tweezer-based assay. · Troponin/tropomyosin regulatory complex; optical tweezers; experiment class: force_generation_motor, receptor_ligand_adhesion
unmapped

Conflicts

No conflicts found among comparable evidence.

42 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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