5ctq

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ctq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ctq OCA], [https://pdbe.org/5ctq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ctq RCSB], [https://www.ebi.ac.uk/pdbsum/5ctq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ctq ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Squamous cell carcinoma antigen recognized by T-cells 3 (SART3) is a U4/U6 recycling factor as well as a targeting factor of USP4 and USP15. However, the details of how SART3 recognizes these deubiquitinases and how they get subsequently translocated into the nucleus are not known. Here, we present the crystal structures of the SART3 half-a-tetratricopeptide (HAT) repeat domain alone and in complex with the domain present in ubiquitin-specific protease (DUSP)-ubiquitin-like (UBL) domains of ubiquitin specific protease 4 (USP4). The 12 HAT repeats of SART3 are in two sub-domains (HAT-N and HAT-C) forming a dimer through HAT-C. USP4 binds SART3 at the opposite surface of the HAT-C dimer interface utilizing the beta-structured linker between the DUSP and the UBL domains. The binding affinities of USP4 and USP15 to SART3 are 0.9 muM and 0.2 muM, respectively. The complex structure of SART3 nuclear localization signal (NLS) and importin-alpha reveals bipartite binding, and removal of SART3 NLS prevents the entry of USP4 (and USP15) into the nucleus and abrogates the subsequent deubiquitinase activity of USP4.

Structural basis for recruiting and shuttling of the spliceosomal deubiquitinase USP4 by SART3.,Park JK, Das T, Song EJ, Kim EE Nucleic Acids Res. 2016 Apr 7. pii: gkw218. PMID:27060135<ref>PMID:27060135</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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