2n9e: Difference between revisions
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==Structure of SUMO-2 bound to phosphorylated RAP80 SIM== | |||
<StructureSection load='2n9e' size='340' side='right'caption='[[2n9e]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2n9e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N9E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N9E FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></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=2n9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n9e OCA], [https://pdbe.org/2n9e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n9e RCSB], [https://www.ebi.ac.uk/pdbsum/2n9e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n9e ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Recognition and repair of double stranded DNA breaks (DSB) involves the targeted recruitment of BRCA tumor suppressors to damage foci through binding of both ubiquitin (Ub) and the Ub-like modifier SUMO. RAP80 is a component of the BRCA1 A complex, and plays a key role in the recruitment process through the binding of K63-linked polyUb chains by tandem Ub interacting motifs (UIM). RAP80 also contains a SUMO interacting motif (SIM) just upstream of the tandem UIMs that has been shown to specifically bind the SUMO-2 isoform. The RAP80 tandem UIMs and SIM function collectively for optimal recruitment of BRCA1 to DSBs, though the molecular basis of this process is not well understood. Using NMR spectroscopy, we demonstrate that the RAP80 SIM binds SUMO-2, and that both specificity and affinity are enhanced through phosphorylation of the canonical CK2 site within the SIM. The affinity increase results from an enhancement of electrostatic interactions between the phosphoserines of RAP80 and the SIM recognition module within SUMO-2. The NMR structure of the SUMO-2/phosphoRAP80 complex reveals that the molecular basis for SUMO-2 specificity is due to isoform-specific sequence differences in electrostatic SIM recognition modules. | |||
Molecular Basis for Phosphorylation Dependent SUMO Recognition by the DNA Repair Protein RAP80.,Anamika, Spyracopoulos L J Biol Chem. 2015 Dec 30. pii: jbc.M115.705061. PMID:26719330<ref>PMID:26719330</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 2n9e" style="background-color:#fffaf0;"></div> | ||
[[Category: Anamika | |||
==See Also== | |||
*[[BRCA 3D structures|BRCA 3D structures]] | |||
*[[SUMO 3D Structures|SUMO 3D Structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Anamika A]] | |||
[[Category: Spyracopoulos L]] | |||
Latest revision as of 04:13, 21 November 2024
Structure of SUMO-2 bound to phosphorylated RAP80 SIMStructure of SUMO-2 bound to phosphorylated RAP80 SIM
Structural highlights
Publication Abstract from PubMedRecognition and repair of double stranded DNA breaks (DSB) involves the targeted recruitment of BRCA tumor suppressors to damage foci through binding of both ubiquitin (Ub) and the Ub-like modifier SUMO. RAP80 is a component of the BRCA1 A complex, and plays a key role in the recruitment process through the binding of K63-linked polyUb chains by tandem Ub interacting motifs (UIM). RAP80 also contains a SUMO interacting motif (SIM) just upstream of the tandem UIMs that has been shown to specifically bind the SUMO-2 isoform. The RAP80 tandem UIMs and SIM function collectively for optimal recruitment of BRCA1 to DSBs, though the molecular basis of this process is not well understood. Using NMR spectroscopy, we demonstrate that the RAP80 SIM binds SUMO-2, and that both specificity and affinity are enhanced through phosphorylation of the canonical CK2 site within the SIM. The affinity increase results from an enhancement of electrostatic interactions between the phosphoserines of RAP80 and the SIM recognition module within SUMO-2. The NMR structure of the SUMO-2/phosphoRAP80 complex reveals that the molecular basis for SUMO-2 specificity is due to isoform-specific sequence differences in electrostatic SIM recognition modules. Molecular Basis for Phosphorylation Dependent SUMO Recognition by the DNA Repair Protein RAP80.,Anamika, Spyracopoulos L J Biol Chem. 2015 Dec 30. pii: jbc.M115.705061. PMID:26719330[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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