IL12A binds IL12B

Stable Identifier
Reaction [uncertain]
Homo sapiens
Interleukin-12 subunit alpha binds Interleukin-12 subunit beta by protein disulfide isomerase
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The Interleukin-12 heterodimer (IL-12) is formed by Interleukin-12 subunit alpha (IL12A, IL-12p35) and Interleukin-12 subunit beta (IL12B, IL-12p40) (Podlaski et al. 1992, Kobayashi et al. 1989, Stern et al.1990). Heterodimerization occurs due to charged residue interactions (Yoon et al. 2000) and is stabilized by disulfide bounding.
IL12 heterodimerization is believed to occur in the endoplasmic reticulum (ER) because inhibition of the enzyme Prolyl 4-hydroxylase subunit beta (P4HB), referred to in this article as Protein disulfide isomerase (PDI), by bacitracin causes IL-12 retention in the ER (Alloza & Vandenbroek 2005).

Literature References
PubMed ID Title Journal Year
10899108 Charged residues dominate a unique interlocking topography in the heterodimeric cytokine interleukin-12

Tobin, JF, Yoon, C, Tang, J, Stahl, M, Johnston, SC, Somers, WS

EMBO J 2000
1347984 Molecular characterization of interleukin 12

Stern, AS, Levin, W, Hulmes, JD, Chizzonite, R, Nanduri, VB, Gately, MK, Danho, W, Podlaski, FJ, Pan, YC

Arch. Biochem. Biophys. 1992
15720785 The metallopeptide antibiotic bacitracin inhibits interleukin-12 alphabeta and beta2 secretion

Vandenbroeck, K, Alloza, I

J. Pharm. Pharmacol. 2005
Catalyst Activity

protein disulfide isomerase activity of P4HB [endoplasmic reticulum lumen]

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