4y3b

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of C-terminal modified Tau peptide-hybrid 201D with 14-3-3sigma

Structural highlights

4y3b is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.8Å
Ligands:	,
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

The discovery of novel protein-protein interaction (PPI) modulators represents one of the great molecular challenges of the modern era. PPIs can be modulated by either inhibitor or stabilizer compounds, which target different though proximal regions of the protein interface. In principle, protein-stabilizer complexes can guide the design of PPI inhibitors (and vice versa). In the present work, we combine X-ray crystallographic data from both stabilizer and inhibitor co-crystal complexes of the adapter protein 14-3-3 to characterize, down to the atomic scale, inhibitors of the 14-3-3/Tau PPI, a potential drug target to treat Alzheimer's disease. The most potent compound notably inhibited the binding of phosphorylated full-length Tau to 14-3-3 according to NMR spectroscopy studies. Our work sets a precedent for the rational design of PPI inhibitors guided by PPI stabilizer-protein complexes while potentially enabling access to new synthetically tractable stabilizers of 14-3-3 and other PPIs.

Stabilizer-Guided Inhibition of Protein-Protein Interactions.,Milroy LG, Bartel M, Henen MA, Leysen S, Adriaans JM, Brunsveld L, Landrieu I, Ottmann C Angew Chem Int Ed Engl. 2015 Nov 5. doi: 10.1002/anie.201507976. PMID:26537010^[1]

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

References

↑ Milroy LG, Bartel M, Henen MA, Leysen S, Adriaans JM, Brunsveld L, Landrieu I, Ottmann C. Stabilizer-Guided Inhibition of Protein-Protein Interactions. Angew Chem Int Ed Engl. 2015 Nov 5. doi: 10.1002/anie.201507976. PMID:26537010 doi:http://dx.doi.org/10.1002/anie.201507976

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/4y3b"

@@ Line 1: / Line 1: @@
 ==Crystal structure of C-terminal modified Tau peptide-hybrid 201D with 14-3-3sigma==
-<StructureSection load='4y3b' size='340' side='right' caption='[[4y3b]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<StructureSection load='4y3b' size='340' side='right'caption='[[4y3b]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4y3b]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y3B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y3B FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4y3b]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y3B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y3B FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=49F:(2S)-2-(2-METHOXYETHYL)PYRROLIDINE'>49F</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=49F:(2S)-2-(2-METHOXYETHYL)PYRROLIDINE'>49F</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4y3b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y3b OCA], [http://pdbe.org/4y3b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y3b RCSB], [http://www.ebi.ac.uk/pdbsum/4y3b PDBsum]</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=4y3b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y3b OCA], [https://pdbe.org/4y3b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y3b RCSB], [https://www.ebi.ac.uk/pdbsum/4y3b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y3b ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/1433S_HUMAN 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.
+[https://www.uniprot.org/uniprot/1433S_HUMAN 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.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 19: @@
 </div>
 <div class="pdbe-citations 4y3b" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Microtubule-associated protein 3D structures|Microtubule-associated protein 3D structures]]
+*[[Tau protein 3D structures|Tau protein 3D structures]]
+*[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bartel, M]]
+[[Category: Homo sapiens]]
-[[Category: Brunsveld, L]]
+[[Category: Large Structures]]
-[[Category: Milroy, L G]]
+[[Category: Bartel M]]
-[[Category: Ottmann, C]]
+[[Category: Brunsveld L]]
-[[Category: 14-3-3 fold]]
+[[Category: Milroy LG]]
-[[Category: Adapter protein]]
+[[Category: Ottmann C]]
-[[Category: All alpha-helical]]
-[[Category: Peptide binding protein]]
-[[Category: Protein-protein interaction]]
-[[Category: Signaling protein]]
-[[Category: Tau]]

4y3b

From Proteopedia

Current revision

Crystal structure of C-terminal modified Tau peptide-hybrid 201D with 14-3-3sigma

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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