Reactome | SMAC (DIABLO) forms dimer

SMAC (DIABLO) forms dimer

Stable Identifier

R-HSA-9627106

Type

Reaction [binding]

Species

Homo sapiens

Compartment

cytosol

ReviewStatus

5/5

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The crystal structure of SMAC(DIABLO) at 2.2A resolution revealed that it homodimerized through an extensive hydrophobic interface and formed an elongated arch shaped quaternary structure (Chai J et al. 2000). Missense mutations that disrupt SMAC (DIABLO) dimeric interface, abrogated the XIAP‑neutralizing function of SMAC (DIABLO), suggesting that SMAC dimerization is essential for its pro‑apoptotic activity (Chai et al. 2000). SMAC (DIABLO) was also found to adopt a tetrameric assembly in solution (Mastrangelo E et al. 2015).

Literature References

PubMed ID	Title	Journal	Year
17724022	A dimeric Smac/diablo peptide directly relieves caspase-3 inhibition by XIAP. Dynamic and cooperative regulation of XIAP by Smac/Diablo Yin, Q, Gao, Z, Li, YM, Wang, J, Wu, H, Jiang, X, Tian, Y	J. Biol. Chem.	2007
10972280	Structural and biochemical basis of apoptotic activation by Smac/DIABLO Chai, J, Wang, X, Shi, Y, Wu, JW, Du, C, Kyin, S	Nature	2000