This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2mp2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "2mp2" [edit=sysop:move=sysop])
Current revision (07:01, 1 May 2024) (edit) (undo)
 
(7 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 2mp2 is ON HOLD
+
==Solution structure of SUMO dimer in complex with SIM2-3 from RNF4==
 +
<StructureSection load='2mp2' size='340' side='right'caption='[[2mp2]]' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2mp2]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MP2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MP2 FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2mp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mp2 OCA], [https://pdbe.org/2mp2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mp2 RCSB], [https://www.ebi.ac.uk/pdbsum/2mp2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mp2 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/SUMO3_HUMAN SUMO3_HUMAN] Ubiquitin-like protein which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4.<ref>PMID:11451954</ref> <ref>PMID:18538659</ref>
-
Authors: Xu, Y., Plechanovov, A., Simpson, P., Marchant, J., Leidecker, O., Sebastian, K., Hay, R.T., Matthews, S.J.
+
==See Also==
-
 
+
*[[SUMO 3D Structures|SUMO 3D Structures]]
-
Description: Solution structure of SUMO dimer in complex with SIM2-3 from RNF4
+
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Homo sapiens]]
 +
[[Category: Large Structures]]
 +
[[Category: Mus musculus]]
 +
[[Category: Hay RT]]
 +
[[Category: Leidecker O]]
 +
[[Category: Marchant J]]
 +
[[Category: Matthews SJ]]
 +
[[Category: Plechanovov A]]
 +
[[Category: Sebastian K]]
 +
[[Category: Simpson P]]
 +
[[Category: Xu Y]]

Current revision

Solution structure of SUMO dimer in complex with SIM2-3 from RNF4

PDB ID 2mp2

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools