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1H, 13C, 15N NMR resonance assignments and secondary structure determination of the extra-cellular domain from the human proapoptotic TRAIL-R2 death receptor 5 (DR5-ECD)

1H, 13C, 15N NMR resonance assignments and secondary structure determination of the... Death receptors (DR) selectively drive cancer cells to apoptosis upon binding to the Tumor necrosis factor-a-Related Apoptosis-Inducing Ligand (TRAIL). Complex formation induces the oligomerization of the death receptors DR4 (TRAIL-R1) and DR5 (TRAIL-R2) and transduces the apoptogenic signal to their respective death domains, leading to Death Inducing Signaling Complex (DISC) formation, caspase activation and ultimately cell death. Several crystal structures of the ExtraCellular Domain from Death Receptor 5 (DR5-ECD) have been reported in complex with the TRAIL ligand or anti-DR5 antibodies, but none for the isolated protein. In order to fill this gap and to perform binding experiments with TRAIL peptidomimetics, we have produced isotopically labelled DR5-ECD and started a conformational analysis by using high-field 3D NMR spectroscopy. Herein, we present the first resonance assignment of a TRAIL receptor in solution and the determination of its secondary structure from NMR chemical shifts. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biomolecular NMR Assignments Springer Journals

1H, 13C, 15N NMR resonance assignments and secondary structure determination of the extra-cellular domain from the human proapoptotic TRAIL-R2 death receptor 5 (DR5-ECD)

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Publisher
Springer Journals
Copyright
Copyright © 2018 by Springer Nature B.V.
Subject
Physics; Biological and Medical Physics, Biophysics; Polymer Sciences; Biochemistry, general
ISSN
1874-2718
eISSN
1874-270X
DOI
10.1007/s12104-018-9828-1
Publisher site
See Article on Publisher Site

Abstract

Death receptors (DR) selectively drive cancer cells to apoptosis upon binding to the Tumor necrosis factor-a-Related Apoptosis-Inducing Ligand (TRAIL). Complex formation induces the oligomerization of the death receptors DR4 (TRAIL-R1) and DR5 (TRAIL-R2) and transduces the apoptogenic signal to their respective death domains, leading to Death Inducing Signaling Complex (DISC) formation, caspase activation and ultimately cell death. Several crystal structures of the ExtraCellular Domain from Death Receptor 5 (DR5-ECD) have been reported in complex with the TRAIL ligand or anti-DR5 antibodies, but none for the isolated protein. In order to fill this gap and to perform binding experiments with TRAIL peptidomimetics, we have produced isotopically labelled DR5-ECD and started a conformational analysis by using high-field 3D NMR spectroscopy. Herein, we present the first resonance assignment of a TRAIL receptor in solution and the determination of its secondary structure from NMR chemical shifts.

Journal

Biomolecular NMR Assignments – Springer Journals

Published: Jun 5, 2018

References

  • Structural and functional analysis of the interaction between the agonistic monoclonal antibody Apomab and the proapoptotic receptor DR5
    Adams, C; Totpal, K; Lawrence, D; Marsters, S; Pitti, R; Yee, S; Ross, S; Deforge, L; Koeppen, H; Sagolla, M; Compaan, D; Lowman, H; Hymowitz, S; Ashkenazi, A
  • Death receptors: signaling and modulation
    Ashkenazi, A; Dixit, VM
  • Synthetic ligands of death receptor 5 display a cell-selective agonistic effect at different oligomerization levels
    Beyrath, J; Chekkat, N; Smulski, CR; Lombardo, CM; Lechner, MC; Seguin, C; Decossas, M; Spanedda, MV; Frisch, B; Guichard, G; Fournel, S
  • Crystal structure of TRAIL-DR5 complex identifies a critical role of the unique frame insertion in conferring recognition specificity
    Cha, SS; Sung, BJ; Kim, YA; Song, YL; Kim, HJ; Kim, S; Lee, MS; Oh, BH
  • NMRPipe: a multidimensional spectral processing system based on UNIX pipes
    Delaglio, F; Grzesiek, S; Vuister, GW; Zhu, G; Pfeifer, J; Bax, A
  • Molecular recognition by a binary code
    Fellouse, FA; Li, B; Compaan, DM; Peden, AA; Hymowitz, SG; Sidhu, SS
  • Apo2L/TRAIL and the death receptor 5 agonist antibody AMG 655 cooperate to promote receptor clustering and antitumor activity
    Graves, JD; Kordich, JJ; Huang, TH; Piasecki, J; Bush, TL; Sullivan, T; Foltz, IN; Chang, W; Douangpanya, H; Dang, T; O’Neill, JW; Mallari, R; Zhao, X; Branstetter, DG; Rossi, JM; Long, AM; Huang, X; Holland, PM
  • Triggering cell death: the crystal structure of Apo2L/TRAIL in a complex with death receptor 5
    Hymowitz, SG; Christinger, HW; Fuh, G; Ultsch, M; O’Connell, M; Kelley, RF; Ashkenazi, A; Vos, AM
  • Activation of the proapoptotic death receptor DR5 by oligomeric peptide and antiobody agonists
    Li, B; Russell, SJ; Compaan, DM; Totpal, K; Marsters, SA; Ashkenazi, A; Cochran, AG; Hymowitz, SG; Sidhu, SS
  • Identification and molecular cloning of two novel receptors for the cytotoxic ligand TRAIL
    MacFarlane, M; Ahmad, M; Srinivasula, SM; Fernandes-Alnemri, T; Cohen, GM; Alnemri, ES
  • TRAIL in cancer therapy: present and future challenges
    Mérino, D; Lalaoui, N; Morizot, A; Solary, E; Micheau, O
  • Structure of the TRAIL-DR5 complex reveals mechanisms conferring specificity in apoptotic initiation
    Mongkolsapaya, J; Grimes, JM; Chen, N; Xu, XN; Stuart, DI; Jones, EY; Screaton, GR
  • Structure of human cytomegalovirus UL141 binding to TRAIL-R2 reveals novel, non-canonical death receptor interactions
    Nemčovičová, I; Benedict, CA; Zajonc, DM
  • Is TRAIL the holy grail of cancer therapy?
    Newsom-Davis, T; Prieske, S; Walczak, H
  • Multivalent DR5 peptides activate the TRAIL death pathway and exert tumoricidal activity
    Pavet, V; Beyrath, J; Pardin, C; Morizot, A; Lechner, MC; Briand, JP; Wendland, M; Maison, W; Fournel, S; Micheau, O; Guichard, G; Gronemeyer, H
  • Thioether analogues of disulfide-bridged cyclic peptides targeting death receptor 5: conformational analysis, dimerisation and consequences for receptor activation
    Pulka-Ziach, K; Pavet, V; Chekkat, N; Estieu-Gionnet, K; Rohac, R; Lechner, MC; Smulski, CR; Zeder-Lutz, G; Altschuh, D; Gronemeyer, H; Fournel, S; Odaert, B; Guichard, G
  • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    Sattler, M; Schleucher, J; Griesinger, C
  • CcpNmr analysis assign: a flexible platform for integrated NMR analysis
    Skinner, SP; Fogh, RH; Boucher, W; Ragan, TJ; Mureddu, LG; Vuister, GW
  • Targeting death-inducing receptors in cancer therapy
    Takeda, K; Stagg, J; Yagita, H; Okumura, K; Smyth, MJ
  • TRAIL-R2 superoligomerization induced by human monoclobal agonistic antibody KMTR2
    Tamada, T; Shinmi, D; Ikeda, M; Yonezawa, Y; Kataoka, S; Kuroki, R; Mori, E; Motoki, K
  • TRAIL-R2: a novel apoptosis-mediating receptor for TRAIL
    Walczak, H; Degli-Esposti, MA; Johnson, RS; Smolak, PJ; Waugh, JY; Boiani, N; Timour, MS; Gerhart, MJ; Schooley, KA; Smith, CA; Goodwin, RG; Rauch, CT
  • Probability-based protein secondary structure identification using combined NMR chemical-shift data
    Wang, Y; Jardetzky, O
  • 1H, 13C and 15N chemical shift referencing in biomolecular NMR
    Wishart, DS; Bigam, CG; Yao, J; Abildgaard, F; Dyson, HJ; Oldfield, E; Markley, JL; Sykes, BD
  • TALOS-N: protein backbone and sidechain torsion angles predicted from NMR chemical shifts using artificial neural networks
    Yang, S; Bax, A