User:Gregory Hoeprich/Sandbox 1
From Proteopedia
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== Structure/Function Relationships == | == Structure/Function Relationships == | ||
| - | As determined by the '''S'''tructural '''C'''lassification '''o'''f '''P'''rotein's ('''SCOP''') Database, Tropomyosin is categorized as follows (general to specific): | + | As determined by the '''S'''tructural '''C'''lassification '''o'''f '''P'''rotein's ([http://scop.mrc-lmb.cam.ac.uk/scop/| '''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 16:35, 17 April 2011
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| 1c1g, resolution 7.00Å () | |||||||||
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| 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 Protein's (SCOP) Database, Tropomyosin is categorized as follows (general to specific):
- Class: coiled-coil
- Fold: parallel coiled-coil
- Superfamily: tropomyosin
- Family: pig [| 1c1g]
Categorization of Tropomyosin's coiled-coil motif describes a unique pattern of amino acids within the alpha helices that comprise the dimer interface. This pattern is represented as a helical wheel diagram, whereby the four amino acids (two from each alpha chain) that are adjacent to each other contribute to a hydrophobic interaction, while the four amino acids (two from each alpha chain) flanking the hydrophobic core provide an ionic interaction. Both the hydrophobic and ionic interactions contribute to the stability of the dimer. The hydrophobic amino acids from each alpha chain interact with each other in a knobs in holes packing arrangement, whereby the side chain of an amino acid one helix fits in between two amino acid side chains of the adjacent helix.
![Tropomyosin: Coiled-Coil Dimer of two alpha helices (1C1G) [1]](/wiki/index.php/Image:Tropomyosin_Dimer-2.png)
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
