3M7O

Crystal structure of mouse MD-1 in complex with phosphatidylcholine

Summary for 3M7O

• Entry DOI: 10.2210/pdb3m7o/pdb
• Descriptor: Lymphocyte antigen 86, 2-acetamido-2-deoxy-beta-D-glucopyranose, (2S)-3-(octadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate, ... (5 entities in total)
• Functional Keywords: beta sheet, glycoprotein, immunity, inflammatory response, innate immunity, secreted, immune system
• Biological source: Mus musculus (mouse)
• Cellular location: Secreted, extracellular space: O88188
• Total number of polymer chains: 4
• Total formula weight: 76568.54

Authors

Harada, H.,Ohto, U.,Satow, Y. (deposition date: 2010-03-17, release date: 2010-06-09, Last modification date: 2024-10-16)

Primary citation

Harada, H.,Ohto, U.,Satow, Y.
Crystal structure of mouse MD-1 with endogenous phospholipid bound in its cavity
J.Mol.Biol., 400:838-846, 2010

PubMed 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.

PubMed: 20595044
DOI: 10.1016/j.jmb.2010.05.063

Experimental method

X-RAY DIFFRACTION (1.65 Å)