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Structure determination of a tetradecapeptide mimicking the RXVRG consensus sequence recognized by a Xenopus laevis skin endoprotease: An approach based on simulated annealing and 1H NMR

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Summary

The tetradecapeptide of sequence H-Asp-Val-Asp-Glu-Arg 5-Asp-Val-Arg-Gly9-Phe-Ala-Ser-Phe-Leu-NH2 is recognized by a putative maturation endoprotease of the Xenopus laevis skin, which cleaves between Arg8 and Gly9. A conformational search has been performed on this peptide by simulated annealing calculations. Two different models in agreement with the NMR data were found. The conformational difference between the two types of model is located in the consensus sequence, i.e., from Arg5 to Gly9.

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Authors and Affiliations

  1. L.P.C.B., Institut Curie, 11 rue Pierre et Marie Curie, F-75231, Paris Cedex 05, France

    Sonja Meddeb, Jean-Pierre Ballini & Jean-Philippe Demaret

  2. Université Paris VI, 11 rue Pierre et Marie Curie, F-75231, Paris Cedex 05, France

    Sonja Meddeb, Jean-Pierre Ballini & Jean-Philippe Demaret

  3. L.A.S.I.R., C.N.R.S., 2 rue Henry Dunant, F-94320, Thiais, France

    François-Regis Chalaoux & Daniel Baron

  4. Université Paris VI, F-75252, Paris Cedex 05, France

    Daniel Baron & Paul Vigny

  5. C.B.M., C.N.R.S., 1 rue Charles Sadron, F-45071, Orléans Cedex 2, France

    Paul Vigny

Authors
  1. Sonja Meddeb
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  2. François-Regis Chalaoux
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  3. Jean-Pierre Ballini
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  4. Daniel Baron
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  5. Paul Vigny
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  6. Jean-Philippe Demaret
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Meddeb, S., Chalaoux, FR., Ballini, JP. et al. Structure determination of a tetradecapeptide mimicking the RXVRG consensus sequence recognized by a Xenopus laevis skin endoprotease: An approach based on simulated annealing and 1H NMR. J Computer-Aided Mol Des 9, 160–170 (1995). https://doi.org/10.1007/BF00124406

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  • DOI: https://doi.org/10.1007/BF00124406

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