1alu

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1alu, resolution 1.9Å

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HUMAN INTERLEUKIN-6

Contents

Overview

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.

Disease

Known diseases associated with this structure: Kaposi sarcoma, susceptibility to OMIM:[147620], Osteopenia/osteoporosis OMIM:[147620]

About this Structure

1ALU is a Single protein structure of sequence from Homo sapiens with SO4 and TLA as ligands. Full crystallographic information is available from OCA.

Reference

1.9 A crystal structure of interleukin 6: implications for a novel mode of receptor dimerization and signaling., Somers W, Stahl M, Seehra JS, EMBO J. 1997 Mar 3;16(5):989-97. PMID:9118960

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