Identification of Interaction of Proteins LRP1 and NYGGF4 in Alzheimer’s Disease using Computational Tools

Alzheimer’s disease (AD) is characterized by a widespread functional disturbance of the human brain. It may be caused by the deposition of amyloid beta-peptide (Aβ) in plaques in brain tissue. In AD, there is the formation of neurofibrillary tangles containing tau protein, which is proposed to result from an imbalance between the production and clearance of amyloid beta-peptide (Aβ). The degradation and production of Aβ is significantly regulated by low-density lipoprotein receptor-related protein, LRP1, which is a large endocytic receptor. The LRP1 is known to regulate this function by interacting with a novel and specific interactor, NYGGF4 (phosphotyrosine interaction domain containing 1). NYGGF4 is known to be differentially expressed during AD progression. Here, we are trying to computational predict the interaction of LRP1 and NYGGF4 through protein structure prediction and protein-protein interaction.