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![[Figure 1]](jb5033fig1mag.jpg)
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Figure 1
Structure of the cell-death-inducing DFF45-like effector (CIDE) domain in DREP3. (a) Domain organization of CIDE-domain-containing proteins. The location of the CIDE domain is shown. (b) Sequence alignment of various CIDE domains. Previously identified conserved residues involved in hetero-oligomeric and homo-oligomeric complexes are coloured blue for basic residues and red for acidic residues. Secondary structures including α-helices and β-sheets are labelled. DFF40 and DFF45 are from Homo sapiens, while DREP1–DREP4 are from Drosophila melanogaster. (c) Ribbon diagram of the nine molecules of the DREP3 CIDE domain present in the asymmetric unit. The nine molecules are shown separately and are numbered from 1 to 9 according to their average temperature factor. Values in parentheses indicate the average temperature factors. (d) Ribbon diagram of the monomeric structure of the DREP3 CIDE domain. The chain from the N-terminus (N-term) to the C-terminus (C-term) is coloured in a spectrum from blue to red. Helices and sheets are labelled. (e) Structural comparion of all nine molecules detected in the asymmetric unit. The same colour code as used in (c) was used to indicate the superposed molecules. (f) Surface view of the monomeric DREP3 CIDE domain with displayed electrostatics. This is shown in the same view as in (d). |
![[Figure 1]](jb5033fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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