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Conformational dynamics of capping protein and interaction partners : simulation studies.

หน่วยงาน Nanyang Technological University, Singapore

รายละเอียด

ชื่อเรื่อง : Conformational dynamics of capping protein and interaction partners : simulation studies.
นักวิจัย : Lukman, Suryani. , Robinson, Robert C. , Wales, David. , Verma, Chandra S.
คำค้น : DRNTU::Science::Biological sciences.
หน่วยงาน : Nanyang Technological University, Singapore
ผู้ร่วมงาน : -
ปีพิมพ์ : 2554
อ้างอิง : Lukman, S., Robinson, R. C., Wales, D., & Verma, C. S. (2012). Conformational dynamics of capping protein and interaction partners: Simulation studies. Proteins: Structure, Function, and Bioinformatics, 80(4), 1066-1077. , 0887-3585 , http://hdl.handle.net/10220/12220 , http://dx.doi.org/10.1002/prot.24008
ที่มา : -
ความเชี่ยวชาญ : -
ความสัมพันธ์ : Proteins: structure, function, and bioinformatics
ขอบเขตของเนื้อหา : -
บทคัดย่อ/คำอธิบาย :

Capping protein (CP) is important for the regulation of actin polymerization. CP binds to the barbed end of the actin filament and prevents actin polymerization. This interaction is modulated through competitive binding by regulatory proteins such as myotrophin (V-1) and the capping protein interacting (CPI) motif from CARMIL. The binding site of myotrophin overlaps with the region of CP that binds to the barbed end of actin filament, whereas CPI binds at a distant site. The binding of CPI to the myotrophin-CP complex dissociates myotrophin from CP. Detailed multicopy molecular dynamics simulations suggest that the binding of CPI shifts the conformational equilibria of CP away from states that favor myotrophin binding. This shift is underpinned by allosteric effects where CPI inhibits CP through suppression of flexibility and disruption of concerted motions that appear to mediate myotrophin binding. Accompanying these effects are changes in electrostatic interactions, notably those involving residue K142β, which appears to play a critical role in regulating flexibility. In addition, accessibility of the site on CP for binding the key hydrophobic residue W8 of myotrophin is modulated by CPI. These results provide insights into the modulation of CP by CPI and myotrophin and indicate the mechanism by which CPI drives the dissociation of the myotrophin-CP complex. Proteins 2012;. © 2011 Wiley Periodicals, Inc.

บรรณานุกรม :
Lukman, Suryani. , Robinson, Robert C. , Wales, David. , Verma, Chandra S. . (2554). Conformational dynamics of capping protein and interaction partners : simulation studies..
    กรุงเทพมหานคร : Nanyang Technological University, Singapore.
Lukman, Suryani. , Robinson, Robert C. , Wales, David. , Verma, Chandra S. . 2554. "Conformational dynamics of capping protein and interaction partners : simulation studies.".
    กรุงเทพมหานคร : Nanyang Technological University, Singapore.
Lukman, Suryani. , Robinson, Robert C. , Wales, David. , Verma, Chandra S. . "Conformational dynamics of capping protein and interaction partners : simulation studies.."
    กรุงเทพมหานคร : Nanyang Technological University, Singapore, 2554. Print.
Lukman, Suryani. , Robinson, Robert C. , Wales, David. , Verma, Chandra S. . Conformational dynamics of capping protein and interaction partners : simulation studies.. กรุงเทพมหานคร : Nanyang Technological University, Singapore; 2554.