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2017 ; 18
(1
): 206
Nephropedia Template TP
gab.com Text
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English Wikipedia
DisBind: A database of classified functional binding sites in disordered and
structured regions of intrinsically disordered proteins
#MMPMID28381244
Yu JF
; Dou XH
; Sha YJ
; Wang CL
; Wang HB
; Chen YT
; Zhang F
; Zhou Y
; Wang JH
BMC Bioinformatics
2017[Apr]; 18
(1
): 206
PMID28381244
show ga
BACKGROUND: Intrinsically 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. RESULTS: DisBind
(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.
CONCLUSION: The searchable DisBind provides a reliable data resource for
functional classification of intrinsically disordered proteins at the residue
level.