Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/20681
Title: Structural Basis for the Inhibition Mechanism of HUman CSE and a study on c-CBL complexes
Authors: SUN QINGXIANG
Keywords: CSE, c-Cbl, H2S, inhibitor, multiple phosphorylation, structural biology
Issue Date: 18-Aug-2010
Source: SUN QINGXIANG (2010-08-18). Structural Basis for the Inhibition Mechanism of HUman CSE and a study on c-CBL complexes. ScholarBank@NUS Repository.
Abstract: Dysregulation of hydrogen sulfide (H2S), an endogenous gasotransmitter, is associated with various diseases such as hypertension, diabetes mellitus, septic or haemorrhagic shock and pancreatitis. Cystathionine-¿-lyase is the main H2S producing enzyme in the cardiovascular system and is responsible for the above mentioned diseases. Here we report several different crystal structure forms/complexes of human Cystathionine-¿-lyase and relevant biophysical, biochemical studies. This study provides new insights into the inhibition mechanism of production of H2S and insights which will facilitate the structure-based design of novel inhibitors/activators of human Cystathionine-¿-lyase for therapeutic purposes. c-Cbl is an E3 ubiquitin ligase and multi-functional protein that plays a vital role in controlling cell phenotype. Using Surface Plasmon Resonance, we found that multiple phosphorylation in c-Cbl recruiting motif of EGFR and Sprouty2 significantly reduces their binding affinity towards c-Cbl TKB domain. However, the crystal structure displays minimal binding pattern changes. Please refer to the thesis for detailed discussion.
URI: http://scholarbank.nus.edu.sg/handle/10635/20681
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