1ALU

HUMAN INTERLEUKIN-6

Summary for 1ALU

• Entry DOI: 10.2210/pdb1alu/pdb
• Descriptor: INTERLEUKIN-6, SULFATE ION, L(+)-TARTARIC ACID, ... (4 entities in total)
• Functional Keywords: cytokine, interleukin, receptor, signaling, glycoprotein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 21671.49

Authors

Somers, W.S.,Stahl, M.,Seehra, J.S. (deposition date: 1997-06-03, release date: 1998-06-03, Last modification date: 2024-10-23)

Primary citation

Somers, W.,Stahl, M.,Seehra, J.S.
1.9 A crystal structure of interleukin 6: implications for a novel mode of receptor dimerization and signaling.
EMBO J., 16:989-997, 1997

PubMed Abstract: Interleukin 6 (IL-6) has many biological activities in vivo, and deregulation has been implicated in many disease processes. IL-6, a 185 amino acid polypeptide was refolded, purified and crystallized. The crystals diffracted to beyond 1.9 A and the structure was solved using single isomorphous replacement. The X-ray structure of IL-6 is composed of a four helix bundle linked by loops and an additional mini-helix. 157 out of 185 residues are well defined in the final structure, with 18 N-terminal and 8 A-B loop amino acids displaying no interpretable electron density. The three-dimensional structure has been used to construct a model of IL-6 interacting with the IL-6 receptor (alpha-chain) and gp130 (beta-chain) that gives new insight into the process of molecular recognition and signaling. Based on this model, we predict a fourth binding site on IL-6, a low affinity IL-6-IL-6 interaction, which may be necessary for the sequential assembly of a functional hexameric IL-6 receptor complex.

PubMed: 9118960
DOI: 10.1093/emboj/16.5.989

Experimental method

X-RAY DIFFRACTION (1.9 Å)