ridm@nrct.go.th   ระบบคลังข้อมูลงานวิจัยไทย   รายการโปรดที่คุณเลือกไว้

Molecular basis of Bcl-XL-p53 interaction : insights from molecular dynamics simulations

หน่วยงาน Nanyang Technological University, Singapore

รายละเอียด

ชื่อเรื่อง : Molecular basis of Bcl-XL-p53 interaction : insights from molecular dynamics simulations
นักวิจัย : Bharatham, Nagakumar , Chi, Seung-Wook , Yoon, Ho Sup
คำค้น : DRNTU::Science::Biological sciences
หน่วยงาน : Nanyang Technological University, Singapore
ผู้ร่วมงาน : -
ปีพิมพ์ : 2554
อ้างอิง : Bharatham, N., Chi S. W., Yoon, H. S. (2011). Molecular Basis of Bcl-XL-p53 Interaction: Insights from Molecular Dynamics Simulations. PLoS ONE, 6(10), 1-12. , http://hdl.handle.net/10220/7512 , http://dx.doi.org/10.1371/journal.pone.0026014
ที่มา : -
ความเชี่ยวชาญ : -
ความสัมพันธ์ : PLoS one
ขอบเขตของเนื้อหา : -
บทคัดย่อ/คำอธิบาย :

Bcl-XL, an antiapoptotic Bcl-2 family protein, plays a central role in the regulation of the apoptotic pathway. Heterodimerization of the antiapoptotic Bcl-2 family proteins with the proapoptotic family members such as Bad, Bak, Bim and Bid is a crucial step in the apoptotic regulation. In addition to these conventional binding partners, recent evidences reveal that the Bcl-2 family proteins also interact with noncanonical binding partners such as p53. Our previous NMR studies showed that Bcl-XL: BH3 peptide and Bcl-XL: SN15 peptide (a peptide derived from residues S15-N29 of p53) complex structures share similar modes of bindings. To further elucidate the molecular basis of the interactions, here we have employed molecular dynamics simulations coupled with MM/PBSA approach. Bcl-XL and other Bcl-2 family proteins have 4 hydrophobic pockets (p1–p4), which are occupied by four systematically spaced hydrophobic residues (h1–h4) of the proapoptotic Bad and Bak BH3 peptides. We observed that three conserved hydrophobic residues (F19, W23 and L26) of p53 (SN15) peptide anchor into three hydrophobic pockets (p2–p4) of Bcl-XL in a similar manner as BH3 peptide. Our results provide insights into the novel molecular recognition by Bcl-XL with p53.

บรรณานุกรม :
Bharatham, Nagakumar , Chi, Seung-Wook , Yoon, Ho Sup . (2554). Molecular basis of Bcl-XL-p53 interaction : insights from molecular dynamics simulations.
    กรุงเทพมหานคร : Nanyang Technological University, Singapore.
Bharatham, Nagakumar , Chi, Seung-Wook , Yoon, Ho Sup . 2554. "Molecular basis of Bcl-XL-p53 interaction : insights from molecular dynamics simulations".
    กรุงเทพมหานคร : Nanyang Technological University, Singapore.
Bharatham, Nagakumar , Chi, Seung-Wook , Yoon, Ho Sup . "Molecular basis of Bcl-XL-p53 interaction : insights from molecular dynamics simulations."
    กรุงเทพมหานคร : Nanyang Technological University, Singapore, 2554. Print.
Bharatham, Nagakumar , Chi, Seung-Wook , Yoon, Ho Sup . Molecular basis of Bcl-XL-p53 interaction : insights from molecular dynamics simulations. กรุงเทพมหานคร : Nanyang Technological University, Singapore; 2554.