SMAC (DIABLO) forms dimer

Stable Identifier
Reaction [binding]
Homo sapiens
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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
10972280 Structural and biochemical basis of apoptotic activation by Smac/DIABLO

Chai, J, Du, C, Wu, JW, Kyin, S, Wang, X, Shi, Y

Nature 2000
17724022 A dimeric Smac/diablo peptide directly relieves caspase-3 inhibition by XIAP. Dynamic and cooperative regulation of XIAP by Smac/Diablo

Gao, Z, Tian, Y, Wang, J, Yin, Q, Wu, H, Li, YM, Jiang, X

J. Biol. Chem. 2007
Participant Of
Orthologous Events
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