Protein tyrosine phosphatases (PTP) are enzymes that remove phosphate groups from the phosphorylated tyrosine residues in proteins. PTPs are known to be essential regulators of signal transduction pathways. PTPs such as SHP-1, SHP-2, PTP1B, and TCPTP are involved signaling pathways that control cell proliferation and glucose metabolism, and inhibition of their enzymatic activity is being studied for therapeutic applications. However, due to the similarity of their active sites, cross-reactivity of PTP-targeted inhibitors presents a potential drawback. Thus, it is important to understand how these enzymes recognize their substrates and how they interact with various PTP-targeted inhibitors so that selectivity of future small-molecule inhibitors may be improved. Towards this goal, the structure of TCPTP is analyzed with known targets using X-ray crystallography. T-cell protein tyrosine phosphatase (TCPTP) is highly expressed in hematopoietic tissues and is a key regulator in immune cell signaling. Also, TCPTP regulates cellular proliferation through the dephosphorylation of growth factor receptors which signal through the JAK/STAT pathway. Resulting data will be presented that describes the expression, purification, and crystallization methods of TCPTP with PTP inhibitors.

Purification and crystallization of T-cell protein tyrosine phosphatase

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.