Crystal Structure of a Mammalian CTP: Phosphocholine Cytidylyltransferase Catalytic Domain Reveals Novel Active Site Residues within a Highly Conserved Nucleotidyltransferase Fold

Documenti analoghi

• An auto-inhibitory helix in CTP:phosphocholine cytidylyltransferase hijacks the catalytic residue and constrains a pliable, domain-bridging helix pair
  di: Ramezanpour, Mohsen, et al.
  Pubblicazione: (2018)
• Contribution of Each Membrane Binding Domain of the CTP:Phosphocholine Cytidylyltransferase-α Dimer to Its Activation, Membrane Binding, and Membrane Cross-bridging
  di: Taneva, Svetla, et al.
  Pubblicazione: (2008)
• Expansion of the Nucleoplasmic Reticulum Requires the Coordinated Activity of Lamins and CTP:Phosphocholine Cytidylyltransferase α
  di: Gehrig, Karsten, et al.
  Pubblicazione: (2008)
• Structural Basis for Autoinhibition of CTP:Phosphocholine Cytidylyltransferase (CCT), the Regulatory Enzyme in Phosphatidylcholine Synthesis, by Its Membrane-binding Amphipathic Helix
  di: Lee, Jaeyong, et al.
  Pubblicazione: (2014)
• Identification of an 11-residue portion of CTP-phosphocholine cytidylyltransferase that is required for enzyme-membrane interactions.
  di: Yang, J, et al.
  Pubblicazione: (1997)