Death Associated Protein 5: Difference between revisions

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<StructureSection load='3d3m.pdb' size='400' frame='true' side='right' scene='3d3m/Ribbon/2' caption='Human death associated protein 5 C-terminal (PDB code [[3d3m]])' >
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{{STRUCTURE_3d3m|  PDB=3d3m  |  SCENE=3d3m/Com_view/2  }}


===The Crystal Structure of the C-terminal region of Death Associated Protein 5 (DAP5-CTD)===




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===The Crystal Structure of the C-terminal region of Death Associated Protein 5 (DAP5-CTD, [[3d3m]])===
{{ABSTRACT_PUBMED_18722383}}
{{ABSTRACT_PUBMED_18722383}}


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<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.  
<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.  


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[[Category: Dym, O.]]
[[Category: Dym, O.]]
[[Category: Unger, T.]]
[[Category: Unger, T.]]
[[Category: ISPC, Israel Structural Proteomics Center.]]
[[Category: Acetylation]]
[[Category: Acetylation]]
[[Category: Heat repeat domain]]
[[Category: Heat repeat domain]]
[[Category: Initiation factor]]
[[Category: Initiation factor]]
[[Category: Ispc]]
[[Category: Israel structural proteomics center]]
[[Category: ISPC]]
[[Category: ISPC]]
[[Category: Israel Structural Proteomics Center]]
[[Category: Israel Structural Proteomics Center]]
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