1I1R

CRYSTAL STRUCTURE OF A CYTOKINE/RECEPTOR COMPLEX

Summary for 1I1R

• Entry DOI: 10.2210/pdb1i1r/pdb
• Descriptor: INTERLEUKIN-6 RECEPTOR BETA CHAIN, VIRAL IL-6 (3 entities in total)
• Functional Keywords: cytokine-receptor complex, gp130, viral il-6, cytokine
• Biological source: Homo sapiens (human); More
• Cellular location: Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted: P40189
• Total number of polymer chains: 2
• Total formula weight: 55521.30

Authors

Chow, D.,He, X.,Snow, A.L.,Rose-John, S.,Garcia, K.C. (deposition date: 2001-02-02, release date: 2001-03-28, Last modification date: 2024-10-30)

Primary citation

Chow, D.,He, X.,Snow, A.L.,Rose-John, S.,Garcia, K.C.
Structure of an extracellular gp130 cytokine receptor signaling complex.
Science, 291:2150-2150, 2001

PubMed Abstract: The activation of gp130, a shared signal-transducing receptor for a family of cytokines, is initiated by recognition of ligand followed by oligomerization into a higher order signaling complex. Kaposi's sarcoma-associated herpesvirus encodes a functional homolog of human interleukin-6 (IL-6) that activates human gp130. In the 2.4 angstrom crystal structure of the extracellular signaling assembly between viral IL-6 and human gp130, two complexes are cross-linked into a tetramer through direct interactions between the immunoglobulin domain of gp130 and site III of viral IL-6, which is necessary for receptor activation. Unlike human IL-6 (which uses many hydrophilic residues), the viral cytokine largely uses hydrophobic amino acids to contact gp130, which enhances the complementarity of the viral IL-6-gp130 binding interfaces. The cross-reactivity of gp130 is apparently due to a chemical plasticity evident in the amphipathic gp130 cytokine-binding sites.

PubMed: 11251120
DOI: 10.1126/science.1058308

Experimental method

X-RAY DIFFRACTION (2.4 Å)