Literature DB >> 12824317

ESPript/ENDscript: Extracting and rendering sequence and 3D information from atomic structures of proteins.

Patrice Gouet1, Xavier Robert, Emmanuel Courcelle.   

Abstract

The fortran program ESPript was created in 1993, to display on a PostScript figure multiple sequence alignments adorned with secondary structure elements. A web server was made available in 1999 and ESPript has been linked to three major web tools: ProDom which identifies protein domains, PredictProtein which predicts secondary structure elements and NPS@ which runs sequence alignment programs. A web server named ENDscript was created in 2002 to facilitate the generation of ESPript figures containing a large amount of information. ENDscript uses programs such as BLAST, Clustal and PHYLODENDRON to work on protein sequences and such as DSSP, CNS and MOLSCRIPT to work on protein coordinates. It enables the creation, from a single Protein Data Bank identifier, of a multiple sequence alignment figure adorned with secondary structure elements of each sequence of known 3D structure. Similar 3D structures are superimposed in turn with the program PROFIT and a final figure is drawn with BOBSCRIPT, which shows sequence and structure conservation along the Calpha trace of the query. ESPript and ENDscript are available at http://genopole.toulouse.inra.fr/ESPript.

Mesh:

Substances:

Year:  2003        PMID: 12824317      PMCID: PMC168963          DOI: 10.1093/nar/gkg556

Source DB:  PubMed          Journal:  Nucleic Acids Res        ISSN: 0305-1048            Impact factor:   16.971


  19 in total

1.  ESPript: analysis of multiple sequence alignments in PostScript.

Authors:  P Gouet; E Courcelle; D I Stuart; F Métoz
Journal:  Bioinformatics       Date:  1999-04       Impact factor: 6.937

2.  ENDscript: a workflow to display sequence and structure information.

Authors:  Patrice Gouet; Emmanuel Courcelle
Journal:  Bioinformatics       Date:  2002-05       Impact factor: 6.937

3.  ProDom: automated clustering of homologous domains.

Authors:  Florence Servant; Catherine Bru; Sébastien Carrère; Emmanuel Courcelle; Jérĵme Gouzy; David Peyruc; Daniel Kahn
Journal:  Brief Bioinform       Date:  2002-09       Impact factor: 11.622

4.  Crystallography & NMR system: A new software suite for macromolecular structure determination.

Authors:  A T Brünger; P D Adams; G M Clore; W L DeLano; P Gros; R W Grosse-Kunstleve; J S Jiang; J Kuszewski; M Nilges; N S Pannu; R J Read; L M Rice; T Simonson; G L Warren
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  1998-09-01

5.  Knowledge-based protein secondary structure assignment.

Authors:  D Frishman; P Argos
Journal:  Proteins       Date:  1995-12

6.  PHD: predicting one-dimensional protein structure by profile-based neural networks.

Authors:  B Rost
Journal:  Methods Enzymol       Date:  1996       Impact factor: 1.600

7.  An extensively modified version of MolScript that includes greatly enhanced coloring capabilities.

Authors:  R M Esnouf
Journal:  J Mol Graph Model       Date:  1997-04       Impact factor: 2.518

Review 8.  Gapped BLAST and PSI-BLAST: a new generation of protein database search programs.

Authors:  S F Altschul; T L Madden; A A Schäffer; J Zhang; Z Zhang; W Miller; D J Lipman
Journal:  Nucleic Acids Res       Date:  1997-09-01       Impact factor: 16.971

9.  CATH--a hierarchic classification of protein domain structures.

Authors:  C A Orengo; A D Michie; S Jones; D T Jones; M B Swindells; J M Thornton
Journal:  Structure       Date:  1997-08-15       Impact factor: 5.006

10.  CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice.

Authors:  J D Thompson; D G Higgins; T J Gibson
Journal:  Nucleic Acids Res       Date:  1994-11-11       Impact factor: 16.971

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