SHP-1 is a protein tyrosine phosphatase (PTP) that plays an inhibitory role in the cellular immune response. SHP-1 consists of three domains: two N-terminal SH2 domains and the catalytic PTP domain at the C-terminus. SHP-1 down regulates immune signaling through the dephosphorylation of JAK1 kinase on cytokine receptors. This prevents activated JAK1 from phosphorylating STAT thus inhibiting the transcription of genes required for cell viability. There has been recent interest in studying the inhibition of SHP-1 to maintain an active immune response against cancer cells. However, there are other PTPs such as TCPTP, SHP-2, and PTP1B that are structurally similar to SHP-1 and could cross-react with SHP-1 inhibitors. The objective of this study is to investigate how SHP-1 interacts with known targets so as to identify unique contacts within the active site that are not found in other PTPs. We expect that the results from these studies will aid in the development of inhibitors with improved selectivity for SHP-1. Towards this goal, we aim to determine the structure of SHP-1 catalytic domain with known inhibitors through X-ray crystallography.

SHP-1 structural determination with known inhibitors

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.