Literature DB >> 7608747

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.

S Meddeb1, F R Chalaoux, J P Ballini, D Baron, P Vigny, J P Demaret.   

Abstract

The tetradecapeptide of sequence H-Asp-Val-Asp-Glu-Arg5-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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Year:  1995        PMID: 7608747     DOI: 10.1007/BF00124406

Source DB:  PubMed          Journal:  J Comput Aided Mol Des        ISSN: 0920-654X            Impact factor:   3.686


  13 in total

Review 1.  Mammalian subtilisins: the long-sought dibasic processing endoproteases.

Authors:  P J Barr
Journal:  Cell       Date:  1991-07-12       Impact factor: 41.582

2.  Consensus sequence for precursor processing at mono-arginyl sites. Evidence for the involvement of a Kex2-like endoprotease in precursor cleavages at both dibasic and mono-arginyl sites.

Authors:  K Nakayama; T Watanabe; T Nakagawa; W S Kim; M Nagahama; M Hosaka; K Hatsuzawa; K Kondoh-Hashiba; K Murakami
Journal:  J Biol Chem       Date:  1992-08-15       Impact factor: 5.157

3.  Optimization by simulated annealing.

Authors:  S Kirkpatrick; C D Gelatt; M P Vecchi
Journal:  Science       Date:  1983-05-13       Impact factor: 47.728

Review 4.  Endopeptidases and prohormone processing.

Authors:  N J Darby; D G Smyth
Journal:  Biosci Rep       Date:  1990-02       Impact factor: 3.840

Review 5.  Peptides from frog skin.

Authors:  C L Bevins; M Zasloff
Journal:  Annu Rev Biochem       Date:  1990       Impact factor: 23.643

6.  Signal peptidases recognize a structural feature at the cleavage site of secretory proteins.

Authors:  G Duffaud; M Inouye
Journal:  J Biol Chem       Date:  1988-07-25       Impact factor: 5.157

7.  Structural requirement at the cleavage site for efficient processing of the lipoprotein secretory precursor of Escherichia coli.

Authors:  S Inouye; G Duffaud; M Inouye
Journal:  J Biol Chem       Date:  1986-08-25       Impact factor: 5.157

8.  Precursors for peptide hormones share common secondary structures forming features at the proteolytic processing sites.

Authors:  M Rholam; P Nicolas; P Cohen
Journal:  FEBS Lett       Date:  1986-10-20       Impact factor: 4.124

9.  Xenopus laevis skin Arg-Xaa-Val-Arg-Gly-endoprotease. A highly specific protease cleaving after a single arginine of a consensus sequence of peptide hormone precursors.

Authors:  P F Kuks; C Créminon; A M Leseney; J Bourdais; A Morel; P Cohen
Journal:  J Biol Chem       Date:  1989-09-05       Impact factor: 5.157

10.  Novel peptide fragments originating from PGLa and the caerulein and xenopsin precursors from Xenopus laevis.

Authors:  B W Gibson; L Poulter; D H Williams; J E Maggio
Journal:  J Biol Chem       Date:  1986-04-25       Impact factor: 5.157

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