Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
NCBI PubMed ID: 19946286Journal NLM ID: 101190261Publisher: London, UK: Nature Publishing Group
Correspondence: ceb27
cam.ac.uk
Institutions: Department of Veterinary Medicine, University of Cambridge, Madingley Road, Cambridge, CB3 OES, UK, Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK, Department of Biochemistry, University of Cambridge, 80 Tennis Court Road Cambridge, CB2 1GA, UK
Lipopolysaccharide (LPS), which is produced by Gram-negative bacteria, is a powerful activator of innate immune responses. LPS binds to the proteins Toll-like receptor 4 (TLR4) and MD2 to activate pro-inflammatory signalling pathways. The TLR4-MD2 receptor complex is crucial for the host recognition of Gram-negative bacterial infection, and pathogens have devised many strategies to evade or manipulate TLR4-MD2 activity. The TLR4-MD2 signalling pathway is therefore potentially an important therapeutic target. This Progress article focuses on recent exciting data that have revealed the structural basis of TLR4-MD2 recognition of LPS.
Lipopolysaccharide, immune response, Toll-like receptor 4 (TLR4), Toll-like receptor 4-MD2 complex
Structure type: oligomer
Location inside paper: p.9, fig.1b
Trivial name: lipid IVA, lipid IVa
Compound class: lipid A
Contained glycoepitopes: IEDB_135394,IEDB_135515,IEDB_141807,IEDB_151531
Comments, role: review; lipid IVa, the precursor of E. coli lipid A.
3D data: 3D data
Related record ID(s): 25196, 31989
NCBI Taxonomy refs (TaxIDs): 562
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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