A Large-Scale Structural Classification of Antimicrobial Peptides

Antimicrobial peptides (AMPs) are potent drug candidates against microbial organisms such as bacteria, fungi, parasites, and viruses. AMPs have abundant sequences and structures, two fundamental resources for bioinformatics researches, but analyses on how they associate with each other are either no...

Full description

Saved in:
Bibliographic Details
Published in:BioMed research international 2015-01, Vol.2015 (2015), p.1-6
Main Authors: Lai, Jim Z. C., Yang, Je-Ruei, Lee, Chen-Che, Lee, Hao-Ting, Chang, Kuan Y.
Format: Article
Language:English
Subjects:
Antimicrobial Cationic Peptides - chemistry
Biomedical research
Control
Databases, Protein
Health aspects
Host-parasite relationships
Peptides
Protein Structure, Secondary
Protein Structure, Tertiary
Resource Review
Sequence Homology, Amino Acid
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Antimicrobial peptides (AMPs) are potent drug candidates against microbial organisms such as bacteria, fungi, parasites, and viruses. AMPs have abundant sequences and structures, two fundamental resources for bioinformatics researches, but analyses on how they associate with each other are either nonexistent or limited to partial classification and data. We thus present A Database of Anti-Microbial peptides (ADAM), which contains 7,007 unique sequences and 759 structures, to systematically establish comprehensive associations between AMP sequences and structures through structural folds and to provide an easy access to view their relationships. 30 distinct AMP structural fold clusters with more than one structure are detected and about a thousand AMPs are associated with at least one structural fold cluster. According to ADAM, AMP structural folds are limited—AMPs only cover about 3% of the overall protein fold space.
ISSN:2314-6133
2314-6141
DOI:10.1155/2015/475062