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Domain view: a web tool for protein domain visualization and analysis

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Journal of Structural and Functional Genomics

Abstract

The identification of sequence-based protein domains and their boundaries is often a prelude to structure determination. An accurate prediction of disordered regions, secondary structures and low complexity segments of target protein sequences can improve the efficiency of selection in structural genomics and also aid in design of constructs for directed structural biology studies. At the Center for Eukaryotic Structural Genomics (CESG) we have developed DomainView, a web tool to visualize and analyze predicted protein domains, disordered regions, secondary structures and low complexity segments of target protein sequences for selection of experimental protein structure attempts. DomainView consists of a relational database and a web graphical-user interface. The database was developed based on MySQL, which stores data from target protein sequences and their domains, disordered regions, secondary structures and low complexity segments. The program of the web user interface is a Perl CGI script. When a user searches for a target protein sequence, the script displays the combinational information about the domains and other features of that target sequence graphically on a web page by querying the database. The graphical representation for each feature is linked to a web page showing more detailed annotation information or to a new window directly running the corresponding prediction program to show further information about that feature.

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Acknowledgments

We thank CESG IT core staff and other staff who supported this development work by providing computer services and making suggestions. This project is supported by NIH/NIGMS Grant U54 GM074901.

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Correspondence to George N. Phillips Jr..

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Pan, X., Bingman, C.A., Wesenberg, G.E. et al. Domain view: a web tool for protein domain visualization and analysis. J Struct Funct Genomics 11, 241–245 (2010). https://doi.org/10.1007/s10969-010-9097-4

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  • DOI: https://doi.org/10.1007/s10969-010-9097-4

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