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PROSITE documentation PDOC51827 |
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 [2].
The profile we developed covers the entire XTBD domain.
Last update:January 2017 / First entry.
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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 |