Internal interaction changes within the mutation of SLC26A4 STAS domain
- Authors
- Kim, Jae In; Chang, Hyunjoon; Lee, Myeongsang; Na, Sungsoo
- Issue Date
- 16-10월-2018
- Publisher
- ELSEVIER SCIENCE BV
- Keywords
- Pendrin (SLC26A4); PDS; DFNB4; Molecular dynamics; Network analysis
- Citation
- CHEMICAL PHYSICS LETTERS, v.710, pp.226 - 233
- Indexed
- SCIE
SCOPUS
- Journal Title
- CHEMICAL PHYSICS LETTERS
- Volume
- 710
- Start Page
- 226
- End Page
- 233
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/72470
- DOI
- 10.1016/j.cplett.2018.09.002
- ISSN
- 0009-2614
- Abstract
- Pendrin (SLC26A4) is a protein associated with the auditory system. Pendred syndrome (PDS) and DFNB4 are typical auditory disorders caused by mutations in the SLC26A4 STAS domain. We generated an SLC26A4 STAS domain model and six mutated STAS domain models related to PDS, DFNB4, and PDS/DFNB4 by homology modeling. Molecular dynamics simulation was performed to find the equilibration conformation and fluctuation information. Using fluctuation information, we calculated betweenness centrality and edge betweenness to reveal communication between secondary structures of STAS domain. The edge betweenness results showed that mutated models generate communication signals that are less clear than WT models.
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Collections - College of Engineering > Department of Mechanical Engineering > 1. Journal Articles
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