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Physical Model of EGFR and Ras protein using RP‐Rasmol
Author(s) -
Cox Justin,
Ferguson Michael,
Telscow Jenniffer,
Whitehurst Chanelle,
Stubbs Tamica,
Colton Shan,
Herman Tim
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.lb312
Subject(s) - grb2 , signal transduction , lapatinib , epidermal growth factor receptor , erbb3 , microbiology and biotechnology , cell growth , receptor tyrosine kinase , chemistry , cancer research , biology , biochemistry , cancer , receptor , breast cancer , genetics , trastuzumab
The MSOE SMART (Students Modeling A Research Topic) Team Program establishes partnerships between students and research mentors and enables teams to explore the nature of select proteins. The Waddell SMART Team researched and designed physical models using 3D printing technology of two proteins involved in cell division regulation, the Epidermal Growth Factor Receptor (EGFR), and Ras. EGFR, a tyrosine kinase receptor, has an extracellular ligand binding domain that leads to activation of the intracellular kinase signaling pathway. Once activated, EGFR phosphorylates a GRB2/SOS complex that binds to Ras, a regulatory transduction trans‐membrane protein. Ras has a phosphate binding loop that binds to GTP, providing energy for the reaction. Once activated, Ras undergoes a conformational change and signals cell division. Cancer results from uncontrolled cell growth. In some forms of breast cancer, EGFR is overexpressed, leading to tumor formation. A new drug, Lapatinib, may inhibit this excessive cell proliferation by blocking the ATP binding domain of the tyrosine kinase. In many types of cancer, Ras has been mutated, preventing hydrolysis of GTP, and the transduction pathway remains active, signaling for continued cell division, which may lead to tumor formation. Understanding the structure and function of these proteins may lead to further drug development. Supported by a grant from NIH‐NCRR‐SEPA.