Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2ERJ

Crystal structure of the heterotrimeric interleukin-2 receptor in complex with interleukin-2

Summary for 2ERJ
Entry DOI10.2210/pdb2erj/pdb
DescriptorInterleukin-2 receptor alpha chain, 2-acetamido-2-deoxy-beta-D-glucopyranose, Interleukin-2 receptor beta chain, ... (10 entities in total)
Functional Keywordsinterleukin-2, interleukin-2 alpha receptor, interleukin-2 beta receptor, interleukin-2 gamma receptor, immune system-cytokine complex, immune system/cytokine
Biological sourceHomo sapiens (human)
More
Total number of polymer chains8
Total formula weight196167.43
Authors
Debler, E.W.,Stauber, D.J.,Wilson, I.A. (deposition date: 2005-10-25, release date: 2006-02-21, Last modification date: 2024-10-30)
Primary citationStauber, D.J.,Debler, E.W.,Horton, P.A.,Smith, K.A.,Wilson, I.A.
Crystal structure of the IL-2 signaling complex: Paradigm for a heterotrimeric cytokine receptor.
Proc.Natl.Acad.Sci.Usa, 103:2793-, 2006
Cited by
PubMed Abstract: IL-2 is a cytokine that functions as a growth factor and central regulator in the immune system and mediates its effects through ligand-induced hetero-trimerization of the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c). Here, we describe the crystal structure of the trimeric assembly of the human IL-2 receptor ectodomains in complex with IL-2 at 3.0 A resolution. The quaternary structure is consistent with a stepwise assembly from IL-2/IL-2R alpha to IL-2/IL-2R alpha/IL-2R beta to IL-2/IL-2R alpha/IL-2R beta/gamma(c). The IL-2R alpha subunit forms the largest of the three IL-2/IL-2R interfaces, which, together with the high abundance of charge-charge interactions, correlates well with the rapid association rate and high-affinity interaction of IL-2R alpha with IL-2 at the cell surface. Surprisingly, IL-2R alpha makes no contacts with IL-2R beta or gamma(c), and only minor changes are observed in the IL-2 structure in response to receptor binding. These findings support the principal role of IL-2R alpha to deliver IL-2 to the signaling complex and act as regulator of signal transduction. Cooperativity in assembly of the final quaternary complex is easily explained by the extraordinarily extensive set of interfaces found within the fully assembled IL-2 signaling complex, which nearly span the entire length of the IL-2R beta and gamma(c) subunits. Helix A of IL-2 wedges tightly between IL-2R beta and gamma(c) to form a three-way junction that coalesces into a composite binding site for the final gamma(c) recruitment. The IL-2/gamma(c) interface itself exhibits the smallest buried surface and the fewest hydrogen bonds in the complex, which is consistent with its promiscuous use in other cytokine receptor complexes.
PubMed: 16477002
DOI: 10.1073/pnas.0511161103
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

238895

PDB entries from 2025-07-16

PDB statisticsPDBj update infoContact PDBjnumon