Title : Crystal structure of mouse
MD-1 with endogenous phospholipid bound in its cavity
Abstract :
- 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
Output (sent_index, trigger,
protein,
sugar,
site):
- 1. glycoprotein, , MD-1, -, -
- 1. glycoprotein, , glycoprotein, -, -
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):