Death Associated Protein 5: Difference between revisions

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{{STRUCTURE_3d3m|  PDB=3d3m  |  SCENE=3d3m/Com_view/2  }}  
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===The Crystal Structure of the C-terminal region of Death Associated Protein 5 (DAP5-CTD)===
===The Crystal Structure of the C-terminal region of Death Associated Protein 5 (DAP5-CTD, [[3d3m]])===
 
 
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<StructureSection load='3d3m.pdb' size='500' frame='true' align='right' scene='3d3m/Ribbon/2' >


<scene name='3d3m/Ribbon/5'>Ribbon representation</scene> of a C-terminal domain of human DAP5/p97 (DAP5-CTD) between residues L730 and A897.  FoldIndex predicted unstructured character of the end of the C-terminus (amino acids 899–907) and it is not seen in the structure. The asymmetric unit of DAP5-CTD (3d3m) consists of two independent monomers. Each monomer comprises a globular α-helical HEAT-Repeat (HR) domain consisting of eight helices (rainbow representation), which folds into four HRs: α1α2, α3α4, α5α6, and α7α8. A pair of interacting antiparallel helices linked by a flexible interunit loop forms an HR unit. This fold is widespread in protein–protein interactions (''e.g.'' eIF4GI; ATR, ATM, and TOR families). The boundary of the segment with missing electron density (residues 789–795), which includes the caspase cleavage site between α3 and α4, is marked.  
<scene name='3d3m/Ribbon/5'>Ribbon representation</scene> of a C-terminal domain of human DAP5/p97 (DAP5-CTD) between residues L730 and A897.  FoldIndex predicted unstructured character of the end of the C-terminus (amino acids 899–907) and it is not seen in the structure. The asymmetric unit of DAP5-CTD (3d3m) consists of two independent monomers. Each monomer comprises a globular α-helical HEAT-Repeat (HR) domain consisting of eight helices (rainbow representation), which folds into four HRs: α1α2, α3α4, α5α6, and α7α8. A pair of interacting antiparallel helices linked by a flexible interunit loop forms an HR unit. This fold is widespread in protein–protein interactions (''e.g.'' eIF4GI; ATR, ATM, and TOR families). The boundary of the segment with missing electron density (residues 789–795), which includes the caspase cleavage site between α3 and α4, is marked.  
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