 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](gx5215fig1mag.jpg)
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Figure 1
(a) Sequence alignment of the CARDs from CARD8, NLRP1, Apaf-1 and procaspase-9 (Casp9). The six α-helices of the CARD structures are underlined and are marked above the sequences. The residues that are conserved among the CARDs are shaded yellow and those that are conserved in the CARD8 and NLRP1 CARDS are shaded green. The acidic residues of Apaf-1 CARD that are important for its association with the procaspase-9 CARD are colored red. The acidic residues of CARD8 CARD that form a prominent negatively charged surface patch near the α2–α3 helices are colored red. The basic residues of procaspase-9 that are essential for Apaf-1 binding are colored blue. (b) The MBP-CARD structure is shown as ribbons with MBP colored gray and the CARD colored orange. The six α-helices of the CARD are labeled. The bound maltose at the MBP is shown in stick representation. (c) Details of the MBP–CARD interface are shown with hydrogen bonds displayed as gray dotted lines. |
![[Figure 1]](gx5215fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
