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  • OER000002503.pdf.jpg
  • Journal article

  • Identification of a new Corin atrial natriuretic peptide-converting enzyme substrate: Agouti-signaling protein (ASIP)

    • Authors : MacDonald, Bryan T.  (2023)

  • Corin is a transmembrane tethered enzyme best known for processing the hormone atrial natriuretic peptide (ANP) in cardiomyocytes to control electrolyte balance and blood pressure. Loss of function mutations in Corin prevent ANP processing and lead to hypertension. Curiously, Corin loss of function variants also result in lighter coat color pigmentation in multiple species. Corin pigmentation effects are dependent on a functional Agouti locus encoding the ago...
  • OER000002615.pdf.jpg
  • Journal article

  • Structural basis for binding of Smaug to the GPCR Smoothened and to the germline inducer Oskar

    • Authors : Kubíková, Jana (2023)

  • Drosophila Smaug and its orthologs comprise a family of mRNA repressor proteins that exhibit various functions during animal development. Smaug proteins contain a characteristic RNA-binding sterile-a motif (SAM) domain and a conserved but uncharacterized N-terminal domain (NTD). Here, we resolved the crystal structure of the NTD of the human SAM domain-containing protein 4A (SAMD4A, a.k.a. Smaug1) to 2.0 Å resolution, which revealed its composi...
  • OER000002435.pdf.jpg
  • Ebooks (Sách điện tử)

  • Understanding ATP binding to DosS catalytic domain with a short ATP-lid

    • Authors : Larson, Grant  (2023)

  • DosS is a heme-sensor histidine kinase that responds to redox-active stimuli in mycobacterial environments by triggering dormancy transformation. Sequence comparison of the catalytic ATP-binding (CA) domain of DosS to other well-studied histidine kinases suggests that it possesses a rather short ATP-lid. This feature has been thought to inhibit DosS kinase activity by blocking ATP binding in the absence of interdomain interactions with the dimerization and histidi...