4ikm

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X-ray structure of CARD8 CARD domain

Structural highlights

4ikm is a 1 chain structure with sequence from Escherichia coli K-12 and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4606Å
Ligands:EDO, GLC, IOD, IYR, PRD_900001, TYI
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.CARD8_HUMAN Inhibits NF-kappa-B activation. May participate in a regulatory mechanism that coordinates cellular responses controlled by NF-kappa-B transcription factor. May be a component of the inflammasome, a protein complex which also includes PYCARD, NALP2 and CASP1 and whose function would be the activation of proinflammatory caspases.

Publication Abstract from PubMed

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 alpha6 helix that is described here for the first time. The surface of the CARD8 CARD displays a prominent acidic patch at its alpha2, alpha3 and alpha5 helices that may interact with the procaspase-9 CARD, whereas an adjacent charged surface at its alpha3 and alpha4 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.

The structure of the CARD8 caspase-recruitment domain suggests its association with the FIIND domain and procaspases through adjacent surfaces.,Jin T, Huang M, Smith P, Jiang J, Xiao TS Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 May;69(Pt 5):482-7. doi:, 10.1107/S1744309113010075. Epub 2013 Apr 27. PMID:23695559[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
2 reviews cite this structure
The versatile roles of CARDs in regulating apoptosis, inflammation, and NF-κB signaling.
Kao et al. (2015)
1 more
6 other articles
No citations found

References

  1. ↑ Jin T, Huang M, Smith P, Jiang J, Xiao TS. The structure of the CARD8 caspase-recruitment domain suggests its association with the FIIND domain and procaspases through adjacent surfaces. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 May;69(Pt 5):482-7. doi:, 10.1107/S1744309113010075. Epub 2013 Apr 27. PMID:23695559 doi:10.1107/S1744309113010075

Contents


PDB ID 4ikm

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OCA

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