LectomeXplore, an update of UniLectin for the discovery of carbohydrate-binding proteins based on a new lectin classification.
Amino Acid Sequence
Animals
Anthozoa
/ genetics
Computational Biology
/ methods
Databases, Protein
Genome
Humans
Internet
Lectins
/ chemistry
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Proteome
/ chemistry
Receptors, Cell Surface
/ chemistry
Sequence Alignment
Sequence Homology, Amino Acid
Software
Terminology as Topic
Journal
Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011
Informations de publication
Date de publication:
08 01 2021
08 01 2021
Historique:
accepted:
16
10
2020
revised:
13
10
2020
received:
15
09
2020
pubmed:
12
11
2020
medline:
27
1
2021
entrez:
11
11
2020
Statut:
ppublish
Résumé
Lectins are non-covalent glycan-binding proteins mediating cellular interactions but their annotation in newly sequenced organisms is lacking. The limited size of functional domains and the low level of sequence similarity challenge usual bioinformatics tools. The identification of lectin domains in proteomes requires the manual curation of sequence alignments based on structural folds. A new lectin classification is proposed. It is built on three levels: (i) 35 lectin domain folds, (ii) 109 classes of lectins sharing at least 20% sequence similarity and (iii) 350 families of lectins sharing at least 70% sequence similarity. This information is compiled in the UniLectin platform that includes the previously described UniLectin3D database of curated lectin 3D structures. Since its first release, UniLectin3D has been updated with 485 additional 3D structures. The database is now complemented by two additional modules: PropLec containing predicted β-propeller lectins and LectomeXplore including predicted lectins from sequences of the NBCI-nr and UniProt for every curated lectin class. UniLectin is accessible at https://www.unilectin.eu/.
Identifiants
pubmed: 33174598
pii: 5974089
doi: 10.1093/nar/gkaa1019
pmc: PMC7778903
doi:
Substances chimiques
Lectins
0
Proteome
0
Receptors, Cell Surface
0
saccharide-binding proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
D1548-D1554Informations de copyright
© The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research.
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