|PROSITE documentation PDOC51827 [for PROSITE entry PS51827]|
XRN2 is an essential eukaryotic exoribonuclease that processes and degrades various substrates. The ~80-residue XRN2-binding domain (XTBD) constitutes an XRN2-binding module that is employed by different metazoan proteins to link to XRN2 [1,2]:
The XTBD domain folds into a globular four-helix bundle (H1-H4) connected by three loops (L1-L3) (see <PDB:5FIR>). H1-H3 form an antiparallel helical array and H4 folds back on top of H2 and H3 at an 90° angle. The four-helical bundle is mainly stabilized by hydrophobic helix-helix interactions together with additional polar interactions between side chains located on neighboring helices. The four-helix bundle of XTBD represents a structurally unique arrangement for XRN2 binding .
The profile we developed covers the entire XTBD domain.Last update:
January 2017 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Miki T.S. Richter H. Rueegger S. Grosshans H.|
|Title||PAXT-1 promotes XRN2 activity by stabilizing it through a conserved domain.|
|Source||Mol. Cell 53:351-360(2014).|
|2||Authors||Richter H. Katic I. Gut H. Grosshans H.|
|Title||Structural basis and function of XRN2 binding by XTB domains.|
|Source||Nat. Struct. Mol. Biol. 23:164-171(2016).|