Tropomyosin

3D Structure of Tropomyosin
The image at the left is a Tropomyosin from Sus scrofa (1c1g).

File:1c1g.png

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Tropomyosin from Sus scrofa, 1c1g
Structural annotation: Resources: InterPro : Ipr000533 Pfam : PF00261 SCOP : d1c1ga_, d1c1gb_, d1c1gc_, d1c1gd_ UniProt : P42639
Functional annotation: Cellular component: cytoskeleton cytoplasm Molecular function: actin binding
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

Tropomyosin

Tropomyosin (TPM) has a 4-helix coiled dimer structure. It regulates the binding of myosin thus regulating muscle contraction. In its locked conformation it binds troponin T (TnnT) and prevents the binding of myosin to actin. When Ca+ atoms bind to TnnT, the TPM assumes an open conformation and myosin can bind to actin. You can enlarge the image at the right for clarity.

3D Structures of Tropomyosin

3mtu, 3mud – cTPM alpha-1 – chicken
1ic2 - cTPM alpha-1 (mutant)
2w49 – cTnnC+cTnnT+cTnnI+cTPM alpha-1+cActin
2z5h – yTPM alpha-1 N-terminal+C-terminal+GNC4+TnnT – yeast
2z5i - yTPM alpha-1 N-terminal+C-terminal+GNC4
2efr, 2efs, 2d3e - rTPM alpha-1 C-terminal+GNC4 – rabbit
1kql - TPM alpha-1 C-terminal+GNC4 - rat
2b9c – TPM mid region – rat
1c1g – TPM – pig
2tma – TPM - model

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Gregory Hoeprich, Alexander Berchansky, David Canner, Joel L. Sussman, Jaime Prilusky, Michal Harel