Title : Essential roles of hydrophobic residues in both MD-2 and toll-like receptor 4 in activation by endotoxin.

Pub. Date : 2009 May 29

PMID : 19321453






2 Functional Relationships(s)
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1 Our mutagenesis studies are consistent with a molecular model in which Val-82, Met-85, and Leu-87 in MD-2 and distal portions of a secondary acyl chain of hexaacylated lipid A that do not fit into the hydrophobic binding pocket of MD-2 form a hydrophobic surface that interacts with Phe-440 and Phe-463 on a neighboring TLR4.MD-2.LPS complex, driving TLR4 activation. Leucine toll like receptor 4 Homo sapiens
2 Our mutagenesis studies are consistent with a molecular model in which Val-82, Met-85, and Leu-87 in MD-2 and distal portions of a secondary acyl chain of hexaacylated lipid A that do not fit into the hydrophobic binding pocket of MD-2 form a hydrophobic surface that interacts with Phe-440 and Phe-463 on a neighboring TLR4.MD-2.LPS complex, driving TLR4 activation. Leucine toll like receptor 4 Homo sapiens