Date of Award
Master of Science in Natural Science
Chemistry and Biochemistry
Dr. Odutayo Odunuga
Dr. Darrell Fry
Dr. Michele Harris
Dr. Josephine Taylor
Striated Muscle UNC-45, also known as UNC-45b, is an important protein that acts as a chaperone for myosin in cardiac and skeletal muscles, binding to myosin at its C-terminal UCS domain and regulating its assembly into thick filaments and sarcomeric structures. The UCS domain contains a large loop that is believed to be the first point of interaction between myosin and UNC-45b. GATA-4 is an essential transcription factor that facilitates transcription of several genes in cardiac development, particularly alpha-heavy chain myosin in heart tissue. Recently, studies have shown that there is interaction of GATA-4 with UNC-45b and that GATA-4 binds to the UCS domain. The implications of this interaction suggests that UNC-45b may play a role in not only the folding of myosin, but in the transcription of it as well. The aim of this study was to identify potential interaction interfaces between GATA-4 and the loop of UNC-45b and determine if the interactions are specific through computational models. Computational analysis suggests that the UCS loop is the preferential binding site of GATA-4 and that van der Waals packing is the primary method of binding.
Duncan, Drake Alexander, "Simulation of the Interaction Between Striated Muscle UNC-45 and Transcription Factor GATA-4" (2021). Electronic Theses and Dissertations. 371.
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