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5mhc

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Revision as of 12:31, 13 March 2019

Crystal structure of 14-3-3sigma and a p53 C-terminal 12-mer synthetic phosphopeptide

Structural highlights

5mhc is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Gene:	SFN, HME1 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[1433S_HUMAN] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway (By similarity). p53-regulated inhibitor of G2/M progression.

Publication Abstract from PubMed

14-3-3 proteins are positive regulators of the tumor suppressor p53, the mutation of which is implicated in many human cancers. Current strategies for targeting of p53 involve restoration of wild-type function or inhibition of the interaction with MDM2, its key negative regulator. Despite the efficacy of these strategies, the alternate approach of stabilizing the interaction of p53 with positive regulators and, thus, enhancing tumor suppressor activity, has not been explored. Here, we report the first example of small-molecule stabilization of the 14-3-3 - p53 protein-protein interaction (PPI) and demonstrate the potential of this approach as a therapeutic modality. We also observed a disconnect between biophysical and crystallographic data in the presence of a stabilizing molecule, which is unusual in 14-3-3 PPIs.

Small-molecule stabilization of the p53 - 14-3-3 protein-protein interaction.,Doveston RG, Kuusk A, Andrei SA, Leysen S, Cao Q, Castaldi MP, Hendricks A, Brunsveld L, Chen H, Boyd H, Ottmann C FEBS Lett. 2017 Aug;591(16):2449-2457. doi: 10.1002/1873-3468.12723. Epub 2017, Aug 6. PMID:28640363^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Doveston RG, Kuusk A, Andrei SA, Leysen S, Cao Q, Castaldi MP, Hendricks A, Brunsveld L, Chen H, Boyd H, Ottmann C. Small-molecule stabilization of the p53 - 14-3-3 protein-protein interaction. FEBS Lett. 2017 Aug;591(16):2449-2457. doi: 10.1002/1873-3468.12723. Epub 2017, Aug 6. PMID:28640363 doi:http://dx.doi.org/10.1002/1873-3468.12723

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5mhc"

@@ Line 1: / Line 1: @@
 ==Crystal structure of 14-3-3sigma and a p53 C-terminal 12-mer synthetic phosphopeptide==
-<StructureSection load='5mhc' size='340' side='right' caption='[[5mhc]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
+<StructureSection load='5mhc' size='340' side='right'caption='[[5mhc]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5mhc]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MHC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MHC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5mhc]] 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=5MHC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MHC FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SFN, HME1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5mhc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mhc OCA], [http://pdbe.org/5mhc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mhc RCSB], [http://www.ebi.ac.uk/pdbsum/5mhc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mhc ProSAT]</span></td></tr>
 </table>
@@ Line 19: / Line 20: @@
 </div>
 <div class="pdbe-citations 5mhc" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Andrei, S]]
 [[Category: Leysen, S]]

5mhc

From Proteopedia

Revision as of 12:31, 13 March 2019

Crystal structure of 14-3-3sigma and a p53 C-terminal 12-mer synthetic phosphopeptide

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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