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| 001 | 172104 | ||
| 005 | 20210129214357.0 | ||
| 024 | 7 | _ | |a 10.1111/febs.12800 |2 doi |
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| 100 | 1 | _ | |a Bobby, Romel |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Functional implications of large backbone amplitude motions of the glycoprotein 130-binding epitope of interleukin-6 |
| 260 | _ | _ | |a Oxford [u.a.] |c 2014 |b Wiley-Blackwell |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1415696391_4058 |2 PUB:(DE-HGF) |
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| 520 | _ | _ | |a Human interleukin (IL)-6 plays a pivotal role in the immune response, hematopoiesis, the acute-phase response, and inflammation. IL-6 has three distinct receptor epitopes, termed sites I, II, and III, that facilitate the formation of a signaling complex. IL-6 signals via a homodimer of glycoprotein 130 (gp130) after initially forming a heterodimer with the nonsignaling a-receptor [IL-6 a-receptor (IL-6R)] via site I. Here, we present the backbone dynamics of apo-IL-6 as determined by analysis of NMR relaxation data with the extended model-free formalism of Lipari and Szabo. To alleviate significant resonance overlap in the HSQC-type spectra, cell-free protein synthesis was used to selectively 15N-label residues, thereby ensuring a complete set of residue-specific dynamics. The calculated order parameters [square of the generalized model-free order parameter (S2)] showed significant conformational heterogeneity among clusters of residues in IL-6. In particular, the N-terminal region of the long AB-loop, which corresponds spatially to one of the gp130 receptor binding epitopes (i.e. site III), experiences substantial fluctuations along the conformation of the main chain (S2 = 0.3–0.8) that are not observed at the other two epitopes or in other cytokines. Thus, we postulate that dynamic properties of the AB-loop are responsible for inhibiting the interaction of IL-6 with gp130 in the absence of the IL-6R, and that binding of IL-6R at site I shifts the dynamic equilibrium to favor interaction with gp130 at site III. In addition, molecular dynamics simulations corroborated the NMR-derived dynamics, and showed that the BC-loop adopts different substates that possibly play a role in facilitating receptor assembly. |
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| 700 | 1 | _ | |a Robustelli, Paul |0 P:(DE-HGF)0 |b 1 |
| 700 | 1 | _ | |a Kralicek, Andrew V. |0 P:(DE-HGF)0 |b 2 |
| 700 | 1 | _ | |a Mobli, Mehdi |0 P:(DE-HGF)0 |b 3 |
| 700 | 1 | _ | |a King, Glenn F. |0 P:(DE-HGF)0 |b 4 |
| 700 | 1 | _ | |a Grötzinger, Joachim |0 P:(DE-HGF)0 |b 5 |
| 700 | 1 | _ | |a Dingley, Andrew J. |0 P:(DE-HGF)0 |b 6 |e Corresponding Author |
| 773 | _ | _ | |a 10.1111/febs.12800 |g Vol. 281, no. 10, p. 2471 - 2483 |0 PERI:(DE-600)2172518-4 |n 10 |p 2471 - 2483 |t The @FEBS journal |v 281 |y 2014 |x 1742-464X |
| 856 | 4 | _ | |u http://onlinelibrary.wiley.com/doi/10.1111/febs.12800/pdf |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/172104/files/FZJ-2014-05647.pdf |y Restricted |
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