CaspR: a web server for automated molecular replacement using homology modelling.

Details

Serval ID
serval:BIB_32026
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
CaspR: a web server for automated molecular replacement using homology modelling.
Journal
Nucleic Acids Research
Author(s)
Claude J.B., Suhre K., Notredame C., Claverie J.M., Abergel C.
ISSN
1362-4962[electronic]
Publication state
Published
Issued date
2004
Volume
32
Number
Web Server issue
Pages
W606-W609
Language
english
Notes
Publication types: Journal Article
Abstract
Molecular replacement (MR) is the method of choice for X-ray crystallography structure determination when structural homologues are available in the Protein Data Bank (PDB). Although the success rate of MR decreases sharply when the sequence similarity between template and target proteins drops below 35% identical residues, it has been found that screening for MR solutions with a large number of different homology models may still produce a suitable solution where the original template failed. Here we present the web tool CaspR, implementing such a strategy in an automated manner. On input of experimental diffraction data, of the corresponding target sequence and of one or several potential templates, CaspR executes an optimized molecular replacement procedure using a combination of well-established stand-alone software tools. The protocol of model building and screening begins with the generation of multiple structure-sequence alignments produced with T-COFFEE, followed by homology model building using MODELLER, molecular replacement with AMoRe and model refinement based on CNS. As a result, CaspR provides a progress report in the form of hierarchically organized summary sheets that describe the different stages of the computation with an increasing level of detail. For the 10 highest-scoring potential solutions, pre-refined structures are made available for download in PDB format. Results already obtained with CaspR and reported on the web server suggest that such a strategy significantly increases the fraction of protein structures which may be solved by MR. Moreover, even in situations where standard MR yields a solution, pre-refined homology models produced by CaspR significantly reduce the time-consuming refinement process. We expect this automated procedure to have a significant impact on the throughput of large-scale structural genomics projects. CaspR is freely available at http://igs-server.cnrs-mrs.fr/Caspr/.
Keywords
Escherichia coli Proteins/chemistry, Internet, Models, Molecular, Sequence Alignment, Sequence Analysis, Protein, Software, Structural Homology, Protein, User-Computer Interface
Pubmed
Web of science
Open Access
Yes
Create date
19/11/2007 10:01
Last modification date
20/08/2019 13:17
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