3zo5: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Structure of SENP2-Loop1 in complex with preSUMO-2== | |||
<StructureSection load='3zo5' size='340' side='right' caption='[[3zo5]], [[Resolution|resolution]] 2.15Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3zo5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZO5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZO5 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ulp1_peptidase Ulp1 peptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.68 3.4.22.68] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3zo5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zo5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zo5 RCSB], [http://www.ebi.ac.uk/pdbsum/3zo5 PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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 A 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. | |||
Structural insights into the SENP6 Loop1 structure in complex with SUMO2.,Alegre KO, Reverter D Protein Sci. 2014 Apr;23(4):433-41. doi: 10.1002/pro.2425. Epub 2014 Mar 10. PMID:24424631<ref>PMID:24424631</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human]] | |||
[[Category: Ulp1 peptidase]] | [[Category: Ulp1 peptidase]] | ||
[[Category: Alegre, K O.]] | [[Category: Alegre, K O.]] | ||
[[Category: Reverter, D.]] | [[Category: Reverter, D.]] | ||
[[Category: Hydrolase-signaling protein complex]] | [[Category: Hydrolase-signaling protein complex]] | ||
Revision as of 13:21, 18 May 2014
Structure of SENP2-Loop1 in complex with preSUMO-2
| ||||||||||||