3qht

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Current revision (11:46, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3qht' size='340' side='right'caption='[[3qht]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='3qht' size='340' side='right'caption='[[3qht]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qht]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [https://en.wikipedia.org/wiki/Synthetic_construct_sequences Synthetic construct sequences]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QHT FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qht]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QHT FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SMT3, YDR510W, D9719.15 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=3qht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qht OCA], [https://pdbe.org/3qht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qht RCSB], [https://www.ebi.ac.uk/pdbsum/3qht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qht ProSAT]</span></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=3qht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qht OCA], [https://pdbe.org/3qht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qht RCSB], [https://www.ebi.ac.uk/pdbsum/3qht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qht ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/SMT3_YEAST SMT3_YEAST]] Not known; suppressor of MIF2 mutations.
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[https://www.uniprot.org/uniprot/SMT3_YEAST SMT3_YEAST] Not known; suppressor of MIF2 mutations.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Discriminating closely related molecules remains a major challenge in the engineering of binding proteins and inhibitors. Here we report the development of highly selective inhibitors of small ubiquitin-related modifier (SUMO) family proteins. SUMOylation is involved in the regulation of diverse cellular processes. Functional differences between two major SUMO isoforms in humans, SUMO1 and SUMO2/3, are thought to arise from distinct interactions mediated by each isoform with other proteins containing SUMO-interacting motifs (SIMs). However, the roles of such isoform-specific interactions are largely uncharacterized due in part to the difficulty in generating high-affinity, isoform-specific inhibitors of SUMO/SIM interactions. We first determined the crystal structure of a "monobody," a designed binding protein based on the fibronectin type III scaffold, bound to the yeast homolog of SUMO. This structure illustrated a mechanism by which monobodies bind to the highly conserved SIM-binding site while discriminating individual SUMO isoforms. Based on this structure, we designed a SUMO-targeted library from which we obtained monobodies that bound to the SIM-binding site of human SUMO1 with K(d) values of approximately 100 nM but bound to SUMO2 400 times more weakly. The monobodies inhibited SUMO1/SIM interactions and, unexpectedly, also inhibited SUMO1 conjugation. These high-affinity and isoform-specific inhibitors will enhance mechanistic and cellular investigations of SUMO biology.
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Isoform-specific monobody inhibitors of small ubiquitin-related modifiers engineered using structure-guided library design.,Gilbreth RN, Truong K, Madu I, Koide A, Wojcik JB, Li NS, Piccirilli JA, Chen Y, Koide S Proc Natl Acad Sci U S A. 2011 May 10;108(19):7751-6. Epub 2011 Apr 25. PMID:21518904<ref>PMID:21518904</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3qht" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[SUMO 3D Structures|SUMO 3D Structures]]
*[[SUMO 3D Structures|SUMO 3D Structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 18824]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Synthetic construct sequences]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Gilbreth, R N]]
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[[Category: Synthetic construct]]
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[[Category: Koide, S]]
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[[Category: Gilbreth RN]]
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[[Category: De novo protein]]
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[[Category: Koide S]]
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[[Category: Fibronectin type iii]]
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[[Category: Smt3]]
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[[Category: Yeast small ubiquitin-like modifier]]
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Current revision

Crystal Structure of the Monobody ySMB-1 bound to yeast SUMO

PDB ID 3qht

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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