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Structure and Dynamics of SARS Coronavirus Proteinase: The Primary Key to the Designing and Screening for Anti-SARS Drugs.

หน่วยงาน สำนักงานพัฒนาวิทยาศาสตร์และเทคโนโลยีแห่งชาติ

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ชื่อเรื่อง : Structure and Dynamics of SARS Coronavirus Proteinase: The Primary Key to the Designing and Screening for Anti-SARS Drugs.
นักวิจัย : Vannajan Sanghiran Lee , Kitiyaporn Wittayanarakul , Tawun Remsungnen , Vudhichai Parasuk , Pornthep Sompompisut , Wasun Chantratita , Chak Sangma , Sornthep Vannarat , Piyaut Srichaikul , Supa Hannongbua , Patchreenart Saparpakorn , Witcha Treesuwan , Ornjira Aruksakulwong , Ekawat Pasomsub , Siriporn Promsri , Daungmanee Chuakheaw , Supot Hannongbua
คำค้น : Artificial Intelligence and signal and image processing , Coronavirus , Information, computing and communication sciences , Molecular dynamics , Molecular structure , Protease , Proteinase , SARS , Simulation and modeling , ศูนย์เทคโนโลยีอิเล็กทรอนิกส์และคอมพิวเตอร์แห่งชาติ
หน่วยงาน : สำนักงานพัฒนาวิทยาศาสตร์และเทคโนโลยีแห่งชาติ
ผู้ร่วมงาน : -
ปีพิมพ์ : 2546
อ้างอิง : http://www.nstda.or.th/thairesearch/node/12844
ที่มา : -
ความเชี่ยวชาญ : -
ความสัมพันธ์ : -
ขอบเขตของเนื้อหา : -
บทคัดย่อ/คำอธิบาย :

Structure and dynamics of SARS coronavirus (SARS-CoV) proteinase have beeninvestigated using molecular dynamics (MD) simulation technique. The simulations werecarried out under the NPT ensemble at 298 K and 1 atm, for free enzyme in both monomer and dimer forms and the monomer-inhibitor complex. The systems were observed to reachequilibrium after 200 ps. Enzyme conformation and its structural changes were monitored interms of root mean square displacement of all 306 amino acid residues. The results show, asexpected, that the proteinase in complex form is, in average, less flexible than the free form.Interest is centered on the two regions, at N-termini (residues 1-2) and around the active site(residues 56-62), in which the flexibilities in complex form is lower than those in free form.This behavior is supposed to facilitate the binding between enzyme and substrate. With theobtained MD structure, molecular dockings have been carried out in order to search for potentSARS-CoV proteinase inhibitors. Preliminary results show that among 16 antiviral drugs takenfrom the NCI database, 4 of them with trade-name Nevirapine, Glycovir, Virazole, and Calanolide A, are observed to fit well in the active site of the SARS-CoV proteinase. /Structure and dynamics of SARS coronavirus (SARS-CoV) proteinase have beeninvestigated using molecular dynamics (MD) simulation technique. The simulations werecarried out under the NPT ensemble at 298 K and 1 atm, for free enzyme in both monomer and dimer forms and the monomer-inhibitor complex. The systems were observed to reachequilibrium after 200 ps. Enzyme conformation and its structural changes were monitored interms of root mean square displacement of all 306 amino acid residues. The results show, asexpected, that the proteinase in complex form is, in average, less flexible than the free form.Interest is centered on the two regions, at N-termini (residues 1-2) and around the active site(residues 56-62), in which the flexibilities in complex form is lower than those in free form.This behavior is supposed to facilitate the binding between enzyme and substrate. With theobtained MD structure, molecular dockings have been carried out in order to search for potentSARS-CoV proteinase inhibitors. Preliminary results show that among 16 antiviral drugs takenfrom the NCI database, 4 of them with trade-name Nevirapine, Glycovir, Virazole, and Calanolide A, are observed to fit well in the active site of the SARS-CoV proteinase.

บรรณานุกรม :
Vannajan Sanghiran Lee , Kitiyaporn Wittayanarakul , Tawun Remsungnen , Vudhichai Parasuk , Pornthep Sompompisut , Wasun Chantratita , Chak Sangma , Sornthep Vannarat , Piyaut Srichaikul , Supa Hannongbua , Patchreenart Saparpakorn , Witcha Treesuwan , Ornjira Aruksakulwong , Ekawat Pasomsub , Siriporn Promsri , Daungmanee Chuakheaw , Supot Hannongbua . (2546). Structure and Dynamics of SARS Coronavirus Proteinase: The Primary Key to the Designing and Screening for Anti-SARS Drugs..
    ปทุมธานี : สำนักงานพัฒนาวิทยาศาสตร์และเทคโนโลยีแห่งชาติ.
Vannajan Sanghiran Lee , Kitiyaporn Wittayanarakul , Tawun Remsungnen , Vudhichai Parasuk , Pornthep Sompompisut , Wasun Chantratita , Chak Sangma , Sornthep Vannarat , Piyaut Srichaikul , Supa Hannongbua , Patchreenart Saparpakorn , Witcha Treesuwan , Ornjira Aruksakulwong , Ekawat Pasomsub , Siriporn Promsri , Daungmanee Chuakheaw , Supot Hannongbua . 2546. "Structure and Dynamics of SARS Coronavirus Proteinase: The Primary Key to the Designing and Screening for Anti-SARS Drugs.".
    ปทุมธานี : สำนักงานพัฒนาวิทยาศาสตร์และเทคโนโลยีแห่งชาติ.
Vannajan Sanghiran Lee , Kitiyaporn Wittayanarakul , Tawun Remsungnen , Vudhichai Parasuk , Pornthep Sompompisut , Wasun Chantratita , Chak Sangma , Sornthep Vannarat , Piyaut Srichaikul , Supa Hannongbua , Patchreenart Saparpakorn , Witcha Treesuwan , Ornjira Aruksakulwong , Ekawat Pasomsub , Siriporn Promsri , Daungmanee Chuakheaw , Supot Hannongbua . "Structure and Dynamics of SARS Coronavirus Proteinase: The Primary Key to the Designing and Screening for Anti-SARS Drugs.."
    ปทุมธานี : สำนักงานพัฒนาวิทยาศาสตร์และเทคโนโลยีแห่งชาติ, 2546. Print.
Vannajan Sanghiran Lee , Kitiyaporn Wittayanarakul , Tawun Remsungnen , Vudhichai Parasuk , Pornthep Sompompisut , Wasun Chantratita , Chak Sangma , Sornthep Vannarat , Piyaut Srichaikul , Supa Hannongbua , Patchreenart Saparpakorn , Witcha Treesuwan , Ornjira Aruksakulwong , Ekawat Pasomsub , Siriporn Promsri , Daungmanee Chuakheaw , Supot Hannongbua . Structure and Dynamics of SARS Coronavirus Proteinase: The Primary Key to the Designing and Screening for Anti-SARS Drugs.. ปทุมธานี : สำนักงานพัฒนาวิทยาศาสตร์และเทคโนโลยีแห่งชาติ; 2546.