PROSITE documentation PDOC51827XRN2-binding (XTBD) domain profile
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]:
- Caenorhabditis elegans Partner of Xrn-Two protein 1, or PAXT-1 for short. Plays a role in maintenance of steady-state concentration and turnover of microRNAs (miRNA) by degradation of mature miRNA in complex with the exoribonuclease XRN-2.
- Mammalian CDKN2A-interacting protein (CDKN2AIP) or Collaborator of ARF (CARF). Regulates DNA damage response in a dose-dependent manner through a number of signaling pathways involved in cell proliferation, apoptosis and senescence.
- Mammalian CDKN2AIP N-terminal-like protein (CDKN2AIPNL).
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 degrees 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 [2].
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). | |
| PubMed ID | 24462208 | |
| DOI | 10.1016/j.molcel.2014.01.001 |
| 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). | |
| PubMed ID | 26779609 | |
| DOI | 10.1038/nsmb.3155 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
View entry in original PROSITE document format
View entry in raw text format (no links)