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Nucleic Acids Res. 2012 Jan;40(Database issue):D507-11. doi: 10.1093/nar/gkr884. Epub 2011 Nov 8.

IDEAL: Intrinsically Disordered proteins with Extensive Annotations and Literature.

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1
Faculty of Engineering, Maebashi Institute of Technology, Maebashi, Gunma 371-0816, Japan. sfukuchi@maebashi-it.ac.jp

Abstract

IDEAL, Intrinsically Disordered proteins with Extensive Annotations and Literature (http://www.ideal.force.cs.is.nagoya-u.ac.jp/IDEAL/), is a collection of knowledge on experimentally verified intrinsically disordered proteins. IDEAL contains manual annotations by curators on intrinsically disordered regions, interaction regions to other molecules, post-translational modification sites, references and structural domain assignments. In particular, IDEAL explicitly describes protean segments that can be transformed from a disordered state to an ordered state. Since in most cases they can act as molecular recognition elements upon binding of partner proteins, IDEAL provides a data resource for functional regions of intrinsically disordered proteins. The information in IDEAL is provided on a user-friendly graphical view and in a computer-friendly XML format.

PMID:
22067451
PMCID:
PMC3245138
DOI:
10.1093/nar/gkr884
[Indexed for MEDLINE]
Free PMC Article
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