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Author Yu, Chin-Sheng ♦ Chen, Jin-Yi ♦ Lu, Chih-Hao ♦ Lin, Yu-Feng
Source Directory of Open Access Journals (DOAJ)
Content type Text
Publisher Hindawi Limited
File Format HTM / HTML
Date Created 2015-09-10
Copyright Year ©2015
Language English
Subject Domain (in LCC) R
Subject Keyword Medicine
Abstract We developed a computational method to identify NAD- and FAD-binding sites in proteins. First, we extracted from the Protein Data Bank structures of proteins that bind to at least one of these ligands. NAD-/FAD-binding residue templates were then constructed by identifying binding residues through the ligand-binding database BioLiP. The fragment transformation method was used to identify structures within query proteins that resembled the ligand-binding templates. By comparing residue types and their relative spatial positions, potential binding sites were identified and a ligand-binding potential for each residue was calculated. Setting the false positive rate at 5%, our method predicted NAD- and FAD-binding sites at true positive rates of 67.1% and 68.4%, respectively. Our method provides excellent results for identifying FAD- and NAD-binding sites in proteins, and the most important is that the requirement of conservation of residue types and local structures in the FAD- and NAD-binding sites can be verified.
ISSN 23146133
Age Range 18 to 22 years ♦ above 22 year
Educational Use Research
Education Level UG and PG ♦ Career/Technical Study
Learning Resource Type Article
Publisher Date 2015-01-01
e-ISSN 23146133
Journal BioMed Research International
Volume Number 2015


Source: Directory of Open Access Journals (DOAJ)