Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/1694
Title: Preliminary report: homology modeling of human ryanodine receptor-1
Other Titles: การทดลองเบื้องต้น: การสร้างแบบจำลองของตัวรับไรยาโนดีน-1 ในมนุษย์โดยใช้เทคนิค Homology Modeling
Authors: Waraphan Toniti
Pranom Puchadapirom
Aekkapot Chamkasem
Mahidol University. Faculty of Veterinary Science. Department of Pre-clinic and Applied Animal Sciences
Mahidol University. Faculty of Science. Department of Pathobiology
Mahidol University. Faculty of Veterinary Science
Keywords: human RyR1;calcium channel;skeletal muscle;Homology modeling;in silico;Open Access article;ตัวรับไรยาโนดีน-1 ในมนุษย์กล้ามเนื้อลาย
Issue Date: 2012
Citation: Journal of Applied Animal Science. Vol.5, No.3 (Sep-Dec 2012), 39-52
Abstract: Excitation-contraction (E-C) coupling is the series of events in which an electrical stimulus is converted into a mechanical contraction. Ryanodine receptors (RyRs), the Ca2+ release channels, located at the sarcoplasmic reticulum membrane and played role in E-C coupling. In this study, human RyR1sequence was studied by sequence of P21817. The in silico RyR1 models were generated using homology modeling. RyR1 is the largest known ion channels and composes of 15 important subdomains; cytoplasmic assembly and transmembrane assembly. This study focused on the larger cytoplasmic assembly that is composed of 10 subdomains. The results show that the shapes and the pocket sites of each domain of RyR1 are different. Each domain has its own pocket sites which facilitateinteraction between RyR1 and modulators. Future studies will certainly resolve additional structural differences among species of interest and may apply as model of calcium release channel-modulator interaction.
URI: http://repository.li.mahidol.ac.th/dspace/handle/123456789/1694
ISSN: 1906-2257
Appears in Collections:VS-Article

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