4IKM

X-ray structure of CARD8 CARD domain

Summary for 4IKM

• Entry DOI: 10.2210/pdb4ikm/pdb
• Related PRD ID: PRD_900001
• Descriptor: Maltose-binding periplasmic protein, Caspase recruitment domain-containing protein 8, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, IODIDE ION, ... (5 entities in total)
• Functional Keywords: death fold superfamily, six-helix bundle, inflammasome, apoptosis, innate immune system, signal transduction, signaling protein
• Biological source: Escherichia coli (human); More
• Total number of polymer chains: 1
• Total formula weight: 54088.30

Authors

Jin, T.,Huang, M.,Smith, P.,Jiang, J.,Xiao, T. (deposition date: 2012-12-26, release date: 2013-05-08, Last modification date: 2024-10-30)

Primary citation

Jin, T.,Huang, M.,Smith, P.,Jiang, J.,Xiao, T.S.
The structure of the CARD8 caspase-recruitment domain suggests its association with the FIIND domain and procaspases through adjacent surfaces.
Acta Crystallogr.,Sect.F, 69:482-487, 2013

PubMed Abstract: 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 α6 helix that is described here for the first time. The surface of the CARD8 CARD displays a prominent acidic patch at its α2, α3 and α5 helices that may interact with the procaspase-9 CARD, whereas an adjacent charged surface at its α3 and α4 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.

PubMed: 23695559
DOI: 10.1107/S1744309113010075

Experimental method

X-RAY DIFFRACTION (2.4606 Å)