Probing the Inflammatory Pathways Associated With Increased Levels of Oxidized LDL Through the Structural Analysis of B17

摘要

The structure of the 17% N-terminal domain of apolipoprotein B-100, apo B-17 (or simply B17), was homology-modeled after the structure of the N-terminus of lipovitellin (LV), a protein that shares not only a sequence homology with B17, but also a functional aspect of lipid binding and transport. The model structure was first forced to accommodate the six disulfide bonds found in that region, and then dynamically relaxed to minimize the free energy of the molecule. The content of secondary structural elements in this model structure correlates excellently with the reported data from other biophysical probes. The C-terminus of B17 shows a considerable homology with a conserved region in the constant domain of the T-cell receptor containing several residues that are essential in the interfacial connectivity with the variable domain. This structural insight may be the first potential link between atherogenic LDL and inflammation.