Publication:
Preliminary report: homology modeling of human ryanodine receptor-1

dc.contributor.authorWaraphan Tonitien_US
dc.contributor.authorPranom Puchadapiromen_US
dc.contributor.authorAekkapot Chamkasemen_US
dc.contributor.otherMahidol University. Faculty of Veterinary Science. Department of Pre-clinic and Applied Animal Sciencesen_US
dc.contributor.otherMahidol University. Faculty of Science. Department of Pathobiologyen_US
dc.contributor.otherMahidol University. Faculty of Veterinary Science
dc.date.accessioned2016-04-26T03:52:50Z
dc.date.accessioned2017-04-10T10:03:26Z
dc.date.available2016-04-26T03:52:50Z
dc.date.available2017-04-10T10:03:26Z
dc.date.created2016-04-26
dc.date.issued2012
dc.description.abstractExcitation-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.en_US
dc.identifier.citationJournal of Applied Animal Science. Vol.5, No.3 (Sep-Dec 2012), 39-52en_US
dc.identifier.issn1906-2257
dc.identifier.urihttps://repository.li.mahidol.ac.th/handle/20.500.14594/1694
dc.language.isoengen_US
dc.rightsMahidol Universityen_US
dc.rights.holderFaculty of Veterinary Science Mahidol Universityen_US
dc.subjecthuman RyR1en_US
dc.subjectcalcium channelen_US
dc.subjectskeletal muscleen_US
dc.subjectHomology modelingen_US
dc.subjectin silicoen_US
dc.subjectOpen Access articleen_US
dc.subjectตัวรับไรยาโนดีน-1 ในมนุษย์กล้ามเนื้อลาย
dc.titlePreliminary report: homology modeling of human ryanodine receptor-1en_US
dc.title.alternativeการทดลองเบื้องต้น: การสร้างแบบจำลองของตัวรับไรยาโนดีน-1 ในมนุษย์โดยใช้เทคนิค Homology Modelingen_US
dc.typeResearch Articleen_US
dspace.entity.typePublication

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