Skip Navigation

This Article
Right arrow FREE Full Text (Print PDF) Freely available
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 ISI Web of Science
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 arrow Search for citing articles in:
ISI Web of Science (47)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Labesse, G.
Right arrow Articles by Mornon, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Labesse, G.
Right arrow Articles by Mornon, J.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Bioinformatics, Vol 14, 206-211, Copyright © 1998 by Oxford University Press


ARTICLES

Incremental threading optimization (TITO) to help alignment and modelling of remote homologues

G Labesse and J Mornon
Systemes Moleculaires et Biologie Structurale, Laboratoire de Mineralogie-Cristallographie, Universites Paris, Cedex, France.

MOTIVATION: Protein sequence comparison has become a major tool for biologists. Various methods have been designed in order to reveal even remote homologies among proteins. Sequence analyses are powerful, but the lower the identity score, the more skill and time are required to perform them accurately. While necessary to confirm the sequence comparison through the potential of mean force, sequence alignment and molecular modelling are still tedious and time-consuming tasks. RESULTS: In order to help sequence threading onto known three- dimensional (3D) structures, we have developed a new program, named TITO (Tool for Incremental Threading Optimization), which uses a multiple alignment to validate and help the refinement of a sequence/structure comparison. It measures the compatibility of a family of related sequences with a known 3D structure. The coordinates of the common core are extracted, allowing further molecular modelling and 3D survey. AVAILABILITY: TITO is available by anonymous ftp at: ftp://lmcp.jussieu. fr/pub/tito CONTACT: labesse@lmcp.jussieu.fr Supplementary information: http://www.lmcp.jussieu.fr/ approximately labesse/TITO/TITO.html
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
Plant Physiol.Home page
E. D. Kouri, N. E. Labrou, S. D. Garbis, K. I. Kalliampakou, C. Stedel, M. Dimou, M. K. Udvardi, P. Katinakis, and E. Flemetakis
Molecular and Biochemical Characterization of the Parvulin-Type PPIases in Lotus japonicus
Plant Physiology, July 1, 2009; 150(3): 1160 - 1173.
[Abstract] [Full Text] [PDF]


Home page
Eukaryot CellHome page
S. Briquet, C. Boschet, M. Gissot, E. Tissandie, E. Sevilla, J.-F. Franetich, I. Thiery, Z. Hamid, C. Bourgouin, and C. Vaquero
High-Mobility-Group Box Nuclear Factors of Plasmodium falciparum.
Eukaryot. Cell, April 1, 2006; 5(4): 672 - 682.
[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
Nucleic Acids ResHome page
F. Allemand, N. Mathy, D. Brechemier-Baey, and C. Condon
The 5S rRNA maturase, ribonuclease M5, is a Toprim domain family member
Nucleic Acids Res., August 2, 2005; 33(13): 4368 - 4376.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. Das, L. Rajagopalan, V. S. Mathura, S. J. Rigby, S. Mitra, and T. K. Hazra
Identification of a Zinc Finger Domain in the Human NEIL2 (Nei-like-2) Protein
J. Biol. Chem., November 5, 2004; 279(45): 47132 - 47138.
[Abstract] [Full Text] [PDF]


Home page
Protein Eng Des SelHome page
N. E. Labrou, G. A. Kotzia, and Y. D. Clonis
Engineering the xenobiotic substrate specificity of maize glutathione S-transferase I
Protein Eng. Des. Sel., October 1, 2004; 17(10): 741 - 748.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
J. Delaunay, G. L. Mee, N. Ezzeddine, G. Labesse, C. Terzian, M. Capri, and O. Ait-Ahmed
The Drosophila Bruno paralogue Bru-3 specifically binds the EDEN translational repression element
Nucleic Acids Res., June 4, 2004; 32(10): 3070 - 3082.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
E. Laurine, D. Lafitte, C. Gregoire, E. Seree, E. Loret, S. Douillard, B. Michel, C. Briand, and J.-M. Verdier
Specific Binding of Dehydroepiandrosterone to the N Terminus of the Microtubule-associated Protein MAP2
J. Biol. Chem., August 8, 2003; 278(32): 29979 - 29986.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J.-L. Pons, F. de Lamotte, M.-F. Gautier, and M.-A. Delsuc
Refined Solution Structure of a Liganded Type 2 Wheat Nonspecific Lipid Transfer Protein
J. Biol. Chem., April 11, 2003; 278(16): 14249 - 14256.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
M. Siaut, C. Zaros, E. Levivier, M.-L. Ferri, M. Court, M. Werner, I. Callebaut, P. Thuriaux, A. Sentenac, and C. Conesa
An Rpb4/Rpb7-Like Complex in Yeast RNA Polymerase III Contains the Orthologue of Mammalian CGRP-RCP
Mol. Cell. Biol., January 1, 2003; 23(1): 195 - 205.
[Abstract] [Full Text]


Home page
Mol Biol EvolHome page
C. Claudianos, J. Brownlie, R. Russell, J. Oakeshott, and S. Whyard
maT--A Clade of Transposons Intermediate Between mariner and Tc1
Mol. Biol. Evol., December 1, 2002; 19(12): 2101 - 2109.
[Abstract] [Full Text] [PDF]


Home page
J. Neurosci.Home page
J. Kniazeff, T. Galvez, G. Labesse, and J.-P. Pin
No Ligand Binding in the GB2 Subunit of the GABAB Receptor Is Required for Activation and Allosteric Interaction between the Subunits
J. Neurosci., September 1, 2002; 22(17): 7352 - 7361.
[Abstract] [Full Text] [PDF]


Home page
Eukaryot CellHome page
C. Dubacq, R. Guerois, R. Courbeyrette, K. Kitagawa, and C. Mann
Sgt1p Contributes to Cyclic AMP Pathway Activity and Physically Interacts with the Adenylyl Cyclase Cyr1p/Cdc35p in Budding Yeast
Eukaryot. Cell, August 1, 2002; 1(4): 568 - 582.
[Abstract] [Full Text] [PDF]


Home page
MicrobiologyHome page
H. Marrakchi, S. Ducasse, G. Labesse, H. Montrozier, E. Margeat, L. Emorine, X. Charpentier, M. Daffe, and A. Quemard
MabA (FabG1), a Mycobacterium tuberculosis protein involved in the long-chain fatty acid elongation system FAS-II
Microbiology, April 1, 2002; 148(4): 951 - 960.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
F. Docagne, N. Colloc'h, V. Bougueret, M. Page, J. Paput, M. Tripier, P. Dutartre, E. T. MacKenzie, A. Buisson, S. Komesli, et al.
A Soluble Transforming Growth Factor-beta (TGF-beta ) Type I Receptor Mimics TGF-beta Responses
J. Biol. Chem., November 30, 2001; 276(49): 46243 - 46250.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
G. Labesse, D. Ferrari, Z.-w. Chen, G.-L. Rossi, V. Kuusk, W. S. McIntire, and F. S. Mathews
Crystallographic and Spectroscopic Studies of Native, Aminoquinol, and Monovalent Cation-bound Forms of Methylamine Dehydrogenase from Methylobacterium extorquens AM1
J. Biol. Chem., October 2, 1998; 273(40): 25703 - 25712.
[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.