HDim1/U5-15kD: Difference between revisions

No edit summary
Line 1: Line 1:
<Structure load='1qgv' size='300' frame='true' align='left' caption='Figure 1: ' scene='Sandbox_502/Hdim1_start_scene/2'/>
== Structure of the hDim1/U5-15kD Protein ==
== Structure of the hDim1/U5-15kD Protein ==
    
    
by Kelly Hrywkiw
by Kelly Hrywkiw
{{STRUCTURE_1qgv |  PDB=1qgv  |  SCENE=  }}
__TOC__
__TOC__


Line 25: Line 25:


==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/2'/>


The thioredoxin-like fold of <scene name='Sandbox_502/Hdim1_start_scene/2'>hDim1</scene> 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 <scene name='Sandbox_502/Hdim1_c-terminal_extension/1'>22 extend the C-terminus</scene>.  This results in an altered structure where β4 and β5 appear to be pulled away from the β-sheet leaving a <scene name='Sandbox_502/Hdim1cleft/1'>cleft</scene> between β3 and β4<ref name ="Reuter"/>.  
The thioredoxin-like fold of <scene name='Sandbox_502/Hdim1_start_scene/2'>hDim1</scene> 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 <scene name='Sandbox_502/Hdim1_c-terminal_extension/1'>22 extend the C-terminus</scene>.  This results in an altered structure where β4 and β5 appear to be pulled away from the β-sheet leaving a <scene name='Sandbox_502/Hdim1cleft/1'>cleft</scene> between β3 and β4<ref name ="Reuter"/>.  

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Kelly Hrywkiw, Alexander Berchansky, Michal Harel