3D Structure, Dimerization Modeling, and Lead Discovery by Ligand-protein Interaction Analysis of p60 Transcription Regulator Protein (p60TRP)
- Authors
- Pramanik, Subrata; Kutzner, Arne; Heese, Klaus
- Issue Date
- Apr-2016
- Publisher
- WILEY-V C H VERLAG GMBH
- Keywords
- BHLHB9; p60TRP; in silico; interaction; lead discovery; brain; Alzheimer' s disease
- Citation
- MOLECULAR INFORMATICS, v.35, no.3-4, pp.99 - 108
- Indexed
- SCIE
SCOPUS
- Journal Title
- MOLECULAR INFORMATICS
- Volume
- 35
- Number
- 3-4
- Start Page
- 99
- End Page
- 108
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/154847
- DOI
- 10.1002/minf.201500035
- ISSN
- 1868-1743
- Abstract
- The p60 transcription regulator protein (p60TRP) is a basic helix-loop-helix (bHLH) domain-containing neuroprotective protein and a member of the G-protein-coupled receptor (GPCR)-associated sorting protein (GPRASP) family. In the present study, multiple theoretical physico-chemical methods (e. g. Modeller v.9.13, I-TASSER, PROCHECK and ClusPro v2.0 with PIPER) were applied to unveil the three-dimensional (3D) protein structure of the p60TRP homodimer protein and explore potential ligand-protein interactions. Our results suggest a Mg2+-containing 3D p60TRP dimer protein that potentially interacts with 5-(1-aziridinyl)-2,4-dinitrobenzamide (CB1954) and [2-(3-dodecylimidazolidin-1-yl)-1-phosphonoethyl] phosphonic acid (B73). The discovery of CB1954 and B73 may serve as a potential lead for further drug screening tests to normalize the p60TRP signaling pathway in neurodegenerative diseases. Interference with p60TRP signaling via CB1954/B73-related molecules might be a novel option for modifying neurodegenerative signaling pathways (e. g. RIN1, PP2A, RanBP5, CREB and SYNJ1) to treat various brain diseases.
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