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Title: Conformational Switch of hRAGE’s Cytoplasmic Domain Upon Protein Self-Association
Authors: اخلاص محمد 
Supervisor: د. جميلة زمون
Keywords: hRAGE’s
Issue Date: 2016
Publisher:  Kuwait university - college of graduate studies
Abstract: iv Abstract The human receptor for advanced glycation end product (hRAGE) is a protein receptor. It has 404 amino acids and consists of three extracellular domains (V, C1 and C2). It also consists of a single transmembrane domain and a cytoplasmic domain. hRAGE is known as a pattern recognition receptor, meaning it is capable of binding a wide variety of ligands. Those ligands include: advanced glycation end products (AGEs), amyloid β peptide, amphoterin and S100 protein family. The cytoplasmic domain, the main focus of this research, is a poorly studied intrinsically disordered region. Understanding the cytoplasmic domain’s behaviors in vitro can add information to help build the complete 3-dimentional structure of hRAGE, which is still unknown. Different modes of self-association, each promoted by a different domain, exist for hRAGE. The self-association into oligomers will be examined using fluorescence spectroscopy, which will examine the environment of the single tryptophan in this domain. These studies showed that the tryptophan 363 switches between two environments according to the protein concentration. The conformational switch is linked to the charge of the neighboring amino acids rather than the polarity of the solvent. Moreover, nuclear magnetic resonance (NMR) is used to test the effect of different concentrations on the behavior of the overall 3- dimensional structure. The conformational switch of the cytoplasmic domain was re-observed, and the self-association of this domain alongside the key amino acids at the self-association interface were identified. Clearly defining the self-association process with this approach will help to understand the detailed structure of hRAGE. This is linked to progress of therapeutic research concerning the pathological complications arising from the over-expression of hRAGE upon ligand binding.
Appears in Programs:0496 Biochemistry

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