Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 69, Issue -, Pages 482-487Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309113010075
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Funding
- National Cancer Institute [Y1-CO-1020]
- National Institute of General Medical Sciences [Y1-GM-1104]
- US Department of Energy [DE-AC02-06CH11357]
- Division of Intramural Research, National Institute of Allergy and Infectious Diseases, NIH
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CARD8 plays crucial roles in regulating apoptotic and inflammatory signaling pathways through the association of its caspase-recruitment domain (CARD) with those of procaspase-9 and procaspase-1. The CARD8 CARD has also been predicted to form an intramolecular complex with its FIIND domain. Here, the first crystal structure of the CARD8 CARD is reported; it adopts a six-helix bundle fold with a unique conformation of the alpha 6 helix that is described here for the first time. The surface of the CARD8 CARD displays a prominent acidic patch at its alpha 2, alpha 3 and alpha 5 helices that may interact with the procaspase-9 CARD, whereas an adjacent charged surface at its alpha 3 and alpha 4 helices may associate with the CARD8 FIIND domain without interfering with the CARD-CARD interaction. This suggests that the function of CARD8 may be regulated by both intramolecular and intermolecular interactions involving electrostatic attractions.
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