Document Detail

Structural basis of the binding of fatty acids to peptidoglycan recognition protein, PGRP-S through second binding site.
MedLine Citation:
PMID:  23149273     Owner:  NLM     Status:  Publisher    
Short peptidoglycan recognition protein (PGRP-S) is a member of the mammalian innate immune system. PGRP-S from Camelus dromedarius (CPGRP-S) has been shown to bind to lipopolysaccharide (LPS), lipoteichoic acid (LTA) and peptidoglycan (PGN). Its structure consists of four molecules A, B, C and D with ligand binding clefts situated at A-B and C-D contacts. It has been shown that LPS, LTA and PGN bind to CPGRP-S at C-D contact. The cleft at the A-B contact indicated features that suggested a possible binding of fatty acids including mycolic acid of Mycobacterium tuberculosis. Therefore, binding studies of CPGRP-S were carried out with fatty acids, butyric acid, lauric acid, myristic acid, stearic acid and mycolic acid which showed affinities in the range of 10(-5)M to 10(-8)M. Structure determinations of the complexes of CPGRP-S with above fatty acids showed that they bound to CPGRP-S in the cleft at the A-B contact. The flow cytometric studies showed that mycolic acid induced the production of pro-inflammatory cytokines, TNF-α and IFN- by CD3+ T cells. The concentrations of cytokines increased considerably with increasing concentrations of mycolic acid. However, their levels decreased substantially on adding CPGRP-S.
Pradeep Sharma; Shavait Yamini; Divya Dube; Amar Singh; Gorakh Mal; Nisha Pandey; Mau Sinha; Abhay Kumar Singh; Sharmistha Dey; Punit Kaur; Dipendra K Mitra; Sujata Sharma; Tej P Singh
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-11-10
Journal Detail:
Title:  Archives of biochemistry and biophysics     Volume:  -     ISSN:  1096-0384     ISO Abbreviation:  Arch. Biochem. Biophys.     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2012-11-14     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0372430     Medline TA:  Arch Biochem Biophys     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2012. Published by Elsevier Inc.
Department of Biophysics, All India Institute of Medical Sciences, New Delhi, India.
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