Dimerization of the Pragmin pseudo-kinase regulates protein tyrosine phosphorylation

Abstract excerpt

<h4>ABSTRACT</h4> The pseudo-kinase and signaling protein Pragmin has been linked to cancer by regulating protein tyrosine phosphorylation via unknown mechanisms. Here we present the crystal structure of the Pragmin 906-1368 amino acids C-terminus, which encompasses its kinase domain. We show that Pragmin contains a classical protein kinase fold devoid of catalytic activity. A particular inhibitory triad, conserv...

Topics

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• Amino Acid Motifs
• CSK Tyrosine-Protein Kinase
• Protein Conformation, alpha-Helical
• Protein Conformation, beta-Strand
• Protein Interaction Domains and Motifs
• Protein Multimerization
• src-Family Kinases
• Tyrosine

Identifiers and source

Literature Corpus work

9f0f7a7c-df87-584f-bd41-de7778437490

DOI

10.1101/218669