Structural highlights
Function
[LY86_MOUSE] May cooperate with CD180 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) and cytokine production. Important for efficient CD180 cell surface expression.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
MD-1 is a glycoprotein that associates with a B-cell-specific RP105 protein and has a low sequence identity of 16% to MD-2 that associates with Toll-like receptor 4 and recognizes endotoxic lipopolysaccharide. MD-1 and RP105 are supposed to mediate lipopolysaccharide recognition; however, little is known about their structures and functions. Here, the crystal structure of mouse MD-1 is determined at 1.65 A resolution. MD-1 has a hydrophobic cavity sandwiched by two beta-sheets as is MD-2. The cavity is 25 A long, 5 A wide, and 10 A deep: longer, narrower, and shallower than that of MD-2. No charged residues are located on the cavity entrance. MD-1 is primarily monomeric in solution but shows a dimeric assembly in the crystal lattices, with their cavity entrances facing each other. In the cavity, electron densities attributable to phosphatidylcholine are located. Together with the binding assay with tetra-acylated lipid IVa, MD-1 is shown to be a lipid-binding coreceptor.
Crystal structure of mouse MD-1 with endogenous phospholipid bound in its cavity.,Harada H, Ohto U, Satow Y J Mol Biol. 2010 Jul 23;400(4):838-46. Epub 2010 Jun 1. PMID:20595044[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gorczynski RM, Chen Z, Clark DA, Hu J, Yu G, Li X, Tsang W, Hadidi S. Regulation of gene expression of murine MD-1 regulates subsequent T cell activation and cytokine production. J Immunol. 2000 Aug 15;165(4):1925-32. PMID:10925274
- ↑ Harada H, Ohto U, Satow Y. Crystal structure of mouse MD-1 with endogenous phospholipid bound in its cavity. J Mol Biol. 2010 Jul 23;400(4):838-46. Epub 2010 Jun 1. PMID:20595044 doi:http://dx.doi.org/10.1016/j.jmb.2010.05.063
