Document Detail


Influence of C-H...O interactions on the structural stability of β-lactamases.
MedLine Citation:
PMID:  23996409     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
P Lavanya; Sudha Ramaiah; Anand Anbarasu
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2013-06-25
Journal Detail:
Title:  Journal of biological physics     Volume:  39     ISSN:  1573-0689     ISO Abbreviation:  J Biol Phys     Publication Date:  2013 Sep 
Date Detail:
Created Date:  2013-09-02     Completed Date:  2014-07-03     Revised Date:  2014-09-02    
Medline Journal Info:
Nlm Unique ID:  0417731     Medline TA:  J Biol Phys     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  649-63     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Binding Sites
Conserved Sequence
Enzyme Stability
Hydrogen Bonding
Models, Molecular
Protein Structure, Secondary
Solvents / chemistry
beta-Lactamases / chemistry*,  metabolism
Chemical
Reg. No./Substance:
0/Solvents; EC 3.5.2.6/beta-Lactamases
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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