Tropomyosin

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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++ ions bind to TnnT, the TPM assumes an open conformation and myosin can bind to actin. The images at the top and at the right correspond to one representative TPM structure, i.e. Tropomyosin from pig (1c1g). You can enlarge the image at the right for clarity.

File:1c1g.png
Crystal Structure of Pig Tropomyosin, 1c1g
Drag the structure with the mouse to rotate
Tropomyosin from pig, 1c1g
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml


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 leucine zipper+TnnT – yeast
2z5i - yTPM alpha-1 N-terminal+C-terminal+GNC4 leucine zipper
2efr, 2efs, 2d3e - rTPM alpha-1 C-terminal+GNC4 leucine zipper – rabbit
1kql - TPM alpha-1 C-terminal+GNC4 leucine zipper - rat
2b9c – TPM mid region – rat
1c1g – TPM – pig
2tma – TPM - model