6XWI

Solution NMR structure of the S0_2.126 designed protein


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 80 
  • Conformers Submitted: 20 
  • Selection Criteria: target function 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

De novo protein design enables the precise induction of RSV-neutralizing antibodies.

Sesterhenn, F.Yang, C.Bonet, J.Cramer, J.T.Wen, X.Wang, Y.Chiang, C.I.Abriata, L.A.Kucharska, I.Castoro, G.Vollers, S.S.Galloux, M.Dheilly, E.Rosset, S.Corthesy, P.Georgeon, S.Villard, M.Richard, C.A.Descamps, D.Delgado, T.Oricchio, E.Rameix-Welti, M.A.Mas, V.Ervin, S.Eleouet, J.F.Riffault, S.Bates, J.T.Julien, J.P.Li, Y.Jardetzky, T.Krey, T.Correia, B.E.

(2020) Science 368

  • DOI: https://doi.org/10.1126/science.aay5051
  • Primary Citation of Related Structures:  
    6S3D, 6VTW, 6XWI, 6XXV

  • PubMed Abstract: 

    De novo protein design has been successful in expanding the natural protein repertoire. However, most de novo proteins lack biological function, presenting a major methodological challenge. In vaccinology, the induction of precise antibody responses remains a cornerstone for next-generation vaccines. Here, we present a protein design algorithm called TopoBuilder, with which we engineered epitope-focused immunogens displaying complex structural motifs. In both mice and nonhuman primates, cocktails of three de novo-designed immunogens induced robust neutralizing responses against the respiratory syncytial virus. Furthermore, the immunogens refocused preexisting antibody responses toward defined neutralization epitopes. Overall, our design approach opens the possibility of targeting specific epitopes for the development of vaccines and therapeutic antibodies and, more generally, will be applicable to the design of de novo proteins displaying complex functional motifs.


  • Organizational Affiliation

    Institute of Bioengineering, École Polytechnique Fédérale de Lausanne, Lausanne CH-1015, Switzerland.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
S0_2.12671synthetic constructMutation(s): 0 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 80 
  • Conformers Submitted: 20 
  • Selection Criteria: target function 

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Swiss National Science FoundationSwitzerland2015/333
European Research Council (ERC)Switzerland716058
Swiss National Science FoundationSwitzerland310030-163139

Revision History  (Full details and data files)

  • Version 1.0: 2020-04-15
    Type: Initial release
  • Version 1.1: 2020-05-06
    Changes: Database references
  • Version 1.2: 2020-05-27
    Changes: Database references
  • Version 1.3: 2023-06-14
    Changes: Database references, Other