Sandbox 502: Difference between revisions
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==Oxidized Full Length Form (hDim1)== | ==Oxidized Full Length Form (hDim1)== | ||
<Structure load='1qgv' size='300' frame='true' align='left' caption='Figure 1: ' scene='Sandbox_502/Hdim1_start_scene/1'/> | |||
The thioredoxin-like fold of hDim1 follows the arrangement of a five stranded β-sheet, consisting of parallel and antiparallel stands, surrounded by three α-helices, where the loop between β4 and α3 could not be resolved. When compared to human thioredoxin there are a total of 37 additional residues in hDim1, which result in several structural differences. For example, the N-terminus is extended by three residues, in the α2-β2 loop one residue is inserted, after β4 nine are inserted, before the α2 helix two are inserted, and 22 extend the C-terminus. This results in an altered structure where β4 and β5 appear to be pulled away from the β-sheet leaving a cleft between β3 and β4. | The thioredoxin-like fold of hDim1 follows the arrangement of a five stranded β-sheet, consisting of parallel and antiparallel stands, surrounded by three α-helices, where the loop between β4 and α3 could not be resolved. When compared to human thioredoxin there are a total of 37 additional residues in hDim1, which result in several structural differences. For example, the N-terminus is extended by three residues, in the α2-β2 loop one residue is inserted, after β4 nine are inserted, before the α2 helix two are inserted, and 22 extend the C-terminus. This results in an altered structure where β4 and β5 appear to be pulled away from the β-sheet leaving a cleft between β3 and β4. | ||
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==Reduced Dominant Negative Form (hDim1-128)== | ==Reduced Dominant Negative Form (hDim1-128)== | ||
<Structure load='1pqn' size='300' frame='true' align='right' caption='Figure 2: ' scene='Sandbox_502/Hdim1-128_start_scene/1'/> | |||
The removal of the C-terminal extension induces cell cycle arrest in G2, however does not affect localization, steady-state levels, or phosphorylation of the protein (Zhang 1999). This suggests that it may be the interactions to other proteins and substrates that are disrupted by the removal of the C-terminal extension (Zhang 1999). It is therefore important to understand the important functional changes the presence of the C-terminal extension creates. | The removal of the C-terminal extension induces cell cycle arrest in G2, however does not affect localization, steady-state levels, or phosphorylation of the protein (Zhang 1999). This suggests that it may be the interactions to other proteins and substrates that are disrupted by the removal of the C-terminal extension (Zhang 1999). It is therefore important to understand the important functional changes the presence of the C-terminal extension creates. | ||
