Influence of C-H...O interactions on the structural stability of β-lactamases

被引:0
作者
P. Lavanya
Sudha Ramaiah
Anand Anbarasu
机构
[1] VIT University,Medical & Biological Computing Laboratory, School of Biosciences and Technology
来源
Journal of Biological Physics | 2013年 / 39卷
关键词
β-lactamases; CH...O interactions; Stabilization centers; Conservation; Solvent accessibility; Secondary structure;
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学科分类号
摘要
β-Lactamases produced by pathogenic bacteria cleave β-lactam antibiotics and render them ineffective. Understanding the principles that govern the structural stability of β-lactamases requires elucidation of the nature of the interactions that are involved in stabilization. In the present study, we systematically analyze the influence of CH...O interactions on determining the specificity and stability of β-lactamases in relation to environmental preferences. It is interesting to note that all the residues located in the active site of β-lactamases are involved in CH...O interactions. A significant percentage of CH...O interactions have a higher conservation score and short-range interactions are the predominant type of interactions in β-lactamases. These results will be useful in understanding the stability patterns of β-lactamases.
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页码:649 / 663
页数:14
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共 190 条
[51]  
Derewenda U(1974)Contribution of polar groups in the interior of a protein to the conformational stability Biochemistry 13 211-14
[52]  
Fabiola GF(2000)Analysis of accessible surface of residues in proteins Structure 8 1319-838
[53]  
Krishnaswamy S(1976)Genetic selection reveals the role of buried, conserved polar residue J. Mol. Biol. 105 1-13
[54]  
Nagarajan V(1985)Amino acid hydrophobicity and accessible surface area Science 229 834-15452
[55]  
Pattabhi V(2007)Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins Protein Sci. 16 4-235
[56]  
Weiss MS(2010)Dramatic structural and thermodynamic consequences of repacking a protein’s hydrophobic core BMC Bioinformatics. 11 286-322
[57]  
Berman HM(2005)The nature of the accessible and buried surfaces in proteins Proc. Natl. Acad. Sci. U.S.A. 102 15447-461
[58]  
Westbrook J(2003)Hydrophobicity of amino acid residues in globular proteins Proteins: Struct. Funct. Genet. 52 225-326
[59]  
Feng Z(2004)Analysis and prediction of functionally important sites in proteins Proteins Struct. Funct. Bioinf. 54 315-1585
[60]  
Gilliland G(2002)Conserved residue clusters at protein–protein interfaces and their use in binding site identification J. Mol. Biol. 323 453-8761