Tropomyosin
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| Tropomyosin from pig, 1c1g | |||||||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
3D Structure of Tropomyosin
The image at the left is a Tropomyosin from pig (1c1g).
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.
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
