DisProt: the database of disordered proteins

被引:633
作者
Sickmeier, Megan
Hamilton, Justin A.
LeGall, Tanguy
Vacic, Vladimir
Cortese, Marc S.
Tantos, Agnes
Szabo, Beata
Tompa, Peter
Chen, Jake
Uversky, Vladimir N.
Obradovic, Zoran
Dunker, A. Keith [1 ]
机构
[1] Indiana Univ, Sch Med, Ctr Computat Biol & Bioinformat, Dept Biochem & Mol Biol, Indianapolis, IN 46202 USA
[2] Univ Calif Riverside, Riverside, CA 92521 USA
[3] Hungarian Acad Sci, Inst Enzymol, Biol Res Ctr, H-1051 Budapest, Hungary
[4] Indiana Univ, Sch Informat, Indianapolis, IN 46202 USA
[5] Temple Univ, Ctr Informat Sci & Technol, Philadelphia, PA 19122 USA
[6] Russian Acad Sci, Inst Biol Instrumentat, Pushchino 142292, Moscow Region, Russia
基金
英国惠康基金; 美国国家卫生研究院;
关键词
D O I
10.1093/nar/gkl893
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The Database of Protein Disorder (DisProt) links structure and function information for intrinsically disordered proteins (IDPs). Intrinsically disordered proteins do not form a fixed three-dimensional structure under physiological conditions, either in their entireties or in segments or regions. We define IDP as a protein that contains at least one experimentally determined disordered region. Although lacking fixed structure, IDPs and regions carry out important biological functions, being typically involved in regulation, signaling and control. Such functions can involve high-specificity low- affinity interactions, the multiple binding of one protein to many partners and the multiple binding of many proteins to one partner. These three features are all enabled and enhanced by protein intrinsic disorder. One of the major hindrances in the study of IDPs has been the lack of organized information. DisProt was developed to enable IDP research by collecting and organizing knowledge regarding the experimental characterization and the functional associations of IDPs. In addition to being a unique source of biological information, DisProt opens doors for a plethora of bioinformatics studies.
引用
收藏
页码:D786 / D793
页数:8
相关论文
共 40 条
[1]   INACTIVATION OF SODIUM CHANNEL .2. GATING CURRENT EXPERIMENTS [J].
ARMSTRONG, CM ;
BEZANILLA, F .
JOURNAL OF GENERAL PHYSIOLOGY, 1977, 70 (05) :567-590
[2]   Comparative genomics and disorder prediction identify biologically relevant SH3 protein interactions [J].
Beltrao, P ;
Serrano, L .
PLOS COMPUTATIONAL BIOLOGY, 2005, 1 (03) :202-211
[3]   Intrinsic disorder is a key characteristic in partners that bind 14-3-3 proteins [J].
Bustos, DM ;
Iglesias, AA .
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2006, 63 (01) :35-42
[4]   The regions of securin and cyclin B proteins recognized by the ubiquitination machinery are natively unfolded [J].
Cox, CJ ;
Dutta, K ;
Petri, ET ;
Hwang, WC ;
Lin, YQ ;
Pascal, SM ;
Basavappa, R .
FEBS LETTERS, 2002, 527 (1-3) :303-308
[5]   The protein trinity - linking function and disorder [J].
Dunker, AK ;
Obradovic, Z .
NATURE BIOTECHNOLOGY, 2001, 19 (09) :805-806
[6]   Intrinsic disorder and protein function [J].
Dunker, AK ;
Brown, CJ ;
Lawson, JD ;
Iakoucheva, LM ;
Obradovic, Z .
BIOCHEMISTRY, 2002, 41 (21) :6573-6582
[7]  
DUNTEN RL, 1989, J BIOL CHEM, V264, P16739
[8]   A practical overview of protein disorder prediction methods [J].
Ferron, Francois ;
Longhi, Sonia ;
Canard, Bruno ;
Karlin, David .
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2006, 65 (01) :1-14
[9]  
Fischer E., 1894, BER DTSCH CHEM GES, V27, P2985, DOI [DOI 10.1002/CBER.18940270364, 10.1002/cber.18940270364]
[10]   Preformed structural elements feature in partner recognition by intrinsically unstructured proteins [J].
Fuxreiter, M ;
Simon, I ;
Friedrich, P ;
Tompa, P .
JOURNAL OF MOLECULAR BIOLOGY, 2004, 338 (05) :1015-1026