Structural insights into the SENP6 Loop1 structure in complex with SUMO2

Kamela O. Alegre, David Reverter

Research output: Contribution to journalArticleResearchpeer-review

7 Citations (Scopus)

Abstract

The SENP proteases regulate the SUMO conjugates in the cell by cleaving SUMO from target proteins. SENP6 and SENP7 are the most divergent members of the SENP/ULP protease family in humans by the presence of insertions in their catalytic domains. Loop1 insertion is determinant for the SUMO2/3 activity and specificity on SENP6 and SENP7. To gain structural insights into the role of Loop1, we have designed a chimeric SENP2 with the insertion of Loop1 into its sequence. The structure of SENP2-Loop1 in complex with SUMO2 was solved at 2.15 Å resolution, and reveals the details of an interface exclusive to SENP6/7 and the formation of unique contacts between both proteins. Interestingly, functional data with SUMO substrates showed an increase of the proteolytic activity in the SENP2-Loop1 chimera for diSUMO2 and polySUMO2 substrates. © 2014 The Protein Society.
Original languageEnglish
Pages (from-to)433-441
JournalProtein Science
Volume23
DOIs
Publication statusPublished - 1 Jan 2014

Keywords

  • PolySUMO chain
  • SENP2
  • SENP6
  • SENP7
  • SUMO
  • Ubiquitin-like protein

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