Tropomyosin
3D Structure of 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++ ions 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.
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| Tropomyosin from pig, 1c1g | |||||||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Tropomyosin
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
Proteopedia Page Contributors and Editors (what is this?)
Gregory Hoeprich, Alexander Berchansky, David Canner, Joel L. Sussman, Jaime Prilusky, Michal Harel
