Skip Navigation


Bioinformatics Advance Access originally published online on July 22, 2004
Bioinformatics 2004 20(18):3694-3696; doi:10.1093/bioinformatics/bth429
This Article
Right arrow FREE Full Text (Print PDF) Freely available
Right arrow FREE Full Text (Screen PDF)
Right arrow All Versions of this Article:
20/18/3694    most recent
bth429v1
Right arrow Comments: Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when Comments are posted
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Catherinot, V.
Right arrow Articles by Labesse, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Catherinot, V.
Right arrow Articles by Labesse, G.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Bioinformatics vol. 20 issue 18 © Oxford University Press 2004; all rights reserved.

Applications Note

ViTO: tool for refinement of protein sequence–structure alignments

Vincent Catherinot * and Gilles Labesse

Centre de Biochimie Structurale, INSERM U414, CNRS UMR5048, Université Montpellier 1 15, Avenue Charles Flahault 34060 Montpellier Cedex, France

Received on June 3, 2004; revised on July 7, 2004; accepted on July 17, 2004
Advance Access Publication July 22, 2004

Summary: ViTO is a graphical application, including an editor, of multiple sequence alignment and a three-dimensional (3D) structure viewer. It is possible to manipulate alignments containing hundreds of sequences and to display a dozen structures. ViTO can handle so-called ‘multiparts’ alignments to allow the visualization of complex structures (multi-chain proteins and/or small molecules and DNA) and the editing of the corresponding alignment. The 3D viewer and the alignment editor are connected together allowing rapid refinement of sequence–structure alignment by taking advantage of the immediate visualization of resulting insertions/deletions and strict conservations in their structural context. More generally, it allows the mapping of informations about the sequence conservation extracted from the alignment onto the 3D structures in a dynamic way. ViTO is also connected to two comparative modelling programs, SCWRL and MODELLER.

These features make ViTO a powerful tool to characterize protein families and to optimize the alignments for comparative modelling.

Availability: http://bioserv.cbs.cnrs.fr/VITO/DOC/

Supplementary information: http://bioserv.cbs.cnrs.fr/VITO/DOC/index.html

Contact: catrino{at}cbs.cnrs.fr

* To whom correspondence should be addressed.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
Nucleic Acids ResHome page
J.-L. Pons and G. Labesse
@TOME-2: a new pipeline for comparative modeling of protein-ligand complexes
Nucleic Acids Res., July 1, 2009; 37(suppl_2): W485 - W491.
[Abstract] [Full Text] [PDF]


Home page
Hum Mol GenetHome page
C. Monnier, C. Dode, L. Fabre, L. Teixeira, G. Labesse, J.-P. Pin, J.-P. Hardelin, and P. Rondard
PROKR2 missense mutations associated with Kallmann syndrome impair receptor signalling activity
Hum. Mol. Genet., January 1, 2009; 18(1): 75 - 81.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
M. Harb, M. M. Becker, D. Vitour, C. H. Baron, P. Vende, S. C. Brown, S. Bolte, S. T. Arold, and D. Poncet
Nuclear Localization of Cytoplasmic Poly(A)-Binding Protein upon Rotavirus Infection Involves the Interaction of NSP3 with eIF4G and RoXaN
J. Virol., November 15, 2008; 82(22): 11283 - 11293.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
P. A. Kaminski, P. Dacher, L. Dugue, and S. Pochet
In Vivo Reshaping the Catalytic Site of Nucleoside 2'-Deoxyribosyltransferase for Dideoxy- and Didehydronucleosides via a Single Amino Acid Substitution
J. Biol. Chem., July 18, 2008; 283(29): 20053 - 20059.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
G. Poncet-Montange, L. Assairi, S. Arold, S. Pochet, and G. Labesse
NAD Kinases Use Substrate-assisted Catalysis for Specific Recognition of NAD
J. Biol. Chem., November 23, 2007; 282(47): 33925 - 33934.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
N. Declerck, L. Bouillaut, D. Chaix, N. Rugani, L. Slamti, F. Hoh, D. Lereclus, and S. T. Arold
Structure of PlcR: Insights into virulence regulation and evolution of quorum sensing in Gram-positive bacteria
PNAS, November 20, 2007; 104(47): 18490 - 18495.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
V. Binet, B. Duthey, J. Lecaillon, C. Vol, J. Quoyer, G. Labesse, J.-P. Pin, and L. Prezeau
Common Structural Requirements for Heptahelical Domain Function in Class A and Class C G Protein-coupled Receptors
J. Biol. Chem., April 20, 2007; 282(16): 12154 - 12163.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
P. Rondard, J. Liu, S. Huang, F. Malhaire, C. Vol, A. Pinault, G. Labesse, and J.-P. Pin
Coupling of Agonist Binding to Effector Domain Activation in Metabotropic Glutamate-like Receptors
J. Biol. Chem., August 25, 2006; 281(34): 24653 - 24661.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
L. Martin, V. Catherinot, and G. Labesse
kinDOCK: a tool for comparative docking of protein kinase ligands.
Nucleic Acids Res., July 1, 2006; 34(Web Server issue): W325 - W329.
[Abstract] [Full Text] [PDF]


Home page
BioinformaticsHome page
W. Li and A. Godzik
VISSA: a program to visualize structural features from structure sequence alignment
Bioinformatics, April 1, 2006; 22(7): 887 - 888.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
L. Ponchon, P. Boulanger, G. Labesse, and L. Letellier
The Endonuclease Domain of Bacteriophage Terminases Belongs to the Resolvase/Integrase/Ribonuclease H Superfamily: A BIOINFORMATICS ANALYSIS VALIDATED BY A FUNCTIONAL STUDY ON BACTERIOPHAGE T5
J. Biol. Chem., March 3, 2006; 281(9): 5829 - 5836.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
E. Hebrard, A. Pinel-Galzi, V. Catherinot, G. Labesse, C. Brugidou, and D. Fargette
Internal Point Mutations of the Capsid Modify the Serotype of Rice Yellow Mottle Virus
J. Virol., April 1, 2005; 79(7): 4407 - 4414.
[Abstract] [Full Text] [PDF]



Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.