Publication: Preliminary report: Homology modeling of Human Ryanodine Receptor-1
Issued Date
2012
Resource Type
Language
eng
ISSN
1906-2257
Rights
Mahidol University
Rights Holder(s)
Faculty of Veterinary Science Mahidol University
Bibliographic Citation
Journal of Applied Animal Science. Vol.5, No.3 (2012), 39-52
Suggested Citation
Waraphan Toniti, Pranom Puchadapirom, Aekkapot Chamkasem Preliminary report: Homology modeling of Human Ryanodine Receptor-1. Journal of Applied Animal Science. Vol.5, No.3 (2012), 39-52. Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/13324
Research Projects
Organizational Units
Authors
Journal Issue
JAAS Vol. 5 No. 3
(2555)
Thesis
Title
Preliminary report: Homology modeling of Human Ryanodine Receptor-1
Alternative Title(s)
การทดลองเบื้องต้น: การสร้างแบบจำลองของตัวรับไรยาโนดีน-1 ในมนุษย์โดยใช้เทคนิค Homology Modeling
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.