Document Detail


Structural features of cholesteryl ester transfer protein: A molecular dynamics simulation study.
MedLine Citation:
PMID:  23042613     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Cholesteryl ester transfer protein (CETP) mediates the net transfer of cholesteryl esters from atheroprotective high-density lipoproteins to atherogenic low-density lipoproteins or very-low-density lipoproteins. Inhibition of CETP raises high-density lipoprotein cholesterol (good cholesterol) levels and reduces low-density lipoprotein cholesterol (bad cholesterol) levels, making it a promising drug target for the prevention and treatment of coronary heart disease. Although the crystal structure of CETP has been determined, the molecular mechanism mediating cholesteryl esters transfer is still unknown, even the structural features of CETP in a physiological environment remain elusive. We performed molecular dynamics simulations to explore the structural features of CETP in an aqueous solution. Results show that the distal portion flexibility of N-terminal β-barrel domain is considerably greater in solution than in crystal; conversely, the flexibility of helix X is slightly less. During the simulations the distal end of C-terminal β-barrel domain expanded while the hydrophilic surface increasing more than the hydrophobic surface. In addition a new surface pore was generated in this domain. This surface pore and all cavities in CETP are stable. These results suggest that the formation of a continuous tunnel within CETP by connecting cavities is permitted in solution. Proteins 2012. © 2012 Wiley Periodicals, Inc.
Authors:
Dongsheng Lei; Xing Zhang; Shengbo Jiang; Zhaodi Cai; Matthew J Rames; Lei Zhang; Gang Ren; Shengli Zhang
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-10-8
Journal Detail:
Title:  Proteins     Volume:  -     ISSN:  1097-0134     ISO Abbreviation:  Proteins     Publication Date:  2012 Oct 
Date Detail:
Created Date:  2012-10-8     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8700181     Medline TA:  Proteins     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2012 Wiley Periodicals, Inc.
Affiliation:
Department of Applied Physics, Xi'an Jiaotong University, Xi'an 710049, People's Republic of China.
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