DisBind: A database of classified functional binding sites in disordered and structured regions of intrinsically disordered proteins

BMC Bioinformatics

Database

Yi-Ting Chen¹  Xiang-Hua Dou¹  Feng Zhang¹  Chun-Ling Wang¹  Yu-Jie Sha²  Jia-Feng Yu²  Hong-Bo Wang²  Ji-Hua Wang³  Yaoqi Zhou⁴ 

[1] College of Physics and Electronic Information, Dezhou University, 253023, Dezhou, China;Shandong Provincial Key Laboratory of Biophysics, Institute of Biophysics, Dezhou University, 253023, Dezhou, China;Shandong Provincial Key Laboratory of Biophysics, Institute of Biophysics, Dezhou University, 253023, Dezhou, China;College of Physics and Electronic Information, Dezhou University, 253023, Dezhou, China;Shandong Provincial Key Laboratory of Biophysics, Institute of Biophysics, Dezhou University, 253023, Dezhou, China;Institute for Glycomics and School of Information and Communication Technology, Griffith University, Parklands Dr, 4222, Southport, QLD, Australia;

关键词: Intrinsic disorder;    Database;    Function classification;    Protein disorder prediction;    Protein function;    Binding site;   

DOI  :  10.1186/s12859-017-1620-1

 received in 2016-08-25, accepted in 2017-03-31,  发布年份 2017

来源: Springer

【 摘 要 】

BackgroundIntrinsically unstructured or disordered proteins function via interacting with other molecules. Annotation of these binding sites is the first step for mapping functional impact of genetic variants in coding regions of human and other genomes, considering that a significant portion of eukaryotic genomes code for intrinsically disordered regions in proteins.ResultsDisBind (available at http://biophy.dzu.edu.cn/DisBind) is a collection of experimentally supported binding sites in intrinsically disordered proteins and proteins with both structured and disordered regions. There are a total of 226 IDPs with functional site annotations. These IDPs contain 465 structured regions (ORs) and 428 IDRs according to annotation by DisProt. The database contains a total of 4232 binding residues (from UniProt and PDB structures) in which 2836 residues are in ORs and 1396 in IDRs. These binding sites are classified according to their interacting partners including proteins, RNA, DNA, metal ions and others with 2984, 258, 383, 350, and 262 annotated binding sites, respectively. Each entry contains site-specific annotations (structured regions, intrinsically disordered regions, and functional binding regions) that are experimentally supported according to PDB structures or annotations from UniProt.ConclusionThe searchable DisBind provides a reliable data resource for functional classification of intrinsically disordered proteins at the residue level.

【 授权许可】

CC BY   
© The Author(s). 2017