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== Structure/Function Relationships ==
== Structure/Function Relationships ==
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As determined by the Structural Classification of Proteins (SCOP) Database, Tropomyosin is categorized as follows (general to specific):
+
As determined by the '''S'''tructural '''C'''lassification '''o'''f '''P'''roteins ('''SCOP''') Database, Tropomyosin is categorized as follows (general to specific):
#'''Class:''' coiled-coil
#'''Class:''' coiled-coil
#'''Fold:''' parallel coiled-coil
#'''Fold:''' parallel coiled-coil

Revision as of 03:23, 17 April 2011

PDB ID 1c1g

Drag the structure with the mouse to rotate
1c1g, resolution 7.00Å ()
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml


Tropomyosin (TM) is an actin binding protein, which consists of a coiled-coil dimer and forms a polymer along the length of actin by a head-to-tail overlap. Its role in muscle mechanics has been well established, but it role in non-muscle systems is becoming evermore clear as there are at least 40 isoforms known in mammals.

Contents

Structure/Function Relationships

As determined by the Structural Classification of Proteins (SCOP) Database, Tropomyosin is categorized as follows (general to specific):

  1. Class: coiled-coil
  2. Fold: parallel coiled-coil
  3. Superfamily: tropomyosin
  4. Family: pig [| 1c1g]

Tropomyosin in Muscle Systems

Tropomyosin in Non-Muscle Systems

Associated Diseases

Evolutionary Conservation

Solved Tropomyosin Structures

3mtu, 3mud – cTPM alpha-1 – chicken
1ic2 - cTPM alpha-1 (mutant)
2w49, 2w4u – 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
1mv4 - TPM alpha-1 C-terminal – rat
2g9j - TPM alpha-1 TM9A+GNC4 – rat
2b9c – TPM mid region – rat
1c1g – TPM – pig
2tma – TPM - model


References

Proteopedia Page Contributors and Editors (what is this?)

Gregory Hoeprich

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