6gkf: Difference between revisions

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~~'''Unreleased structure'''~~

~~The entry~~ 6gkf is ~~ON HOLD until Paper~~ Publication

==Structure of 14-3-3 gamma in complex with caspase-2 14-3-3 binding motif Ser139==

== Structural highlights ==

<table><tr><td colspan='2'>[[6gkf]] is a 16 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=6GKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GKF FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.598Å</td></tr>

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=6gkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gkf OCA], [https://pdbe.org/6gkf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6gkf RCSB], [https://www.ebi.ac.uk/pdbsum/6gkf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6gkf ProSAT]</span></td></tr>

</table>

== Function ==

[https://www.uniprot.org/uniprot/1433G_HUMAN 1433G_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.<ref>PMID:16511572</ref>

== Publication Abstract from PubMed ==

Caspase-2 is an apical protease responsible for the proteolysis of cellular substrates directly involved in mediating apoptotic signaling cascades. Caspase-2 activation is inhibited by phosphorylation followed by binding to the scaffolding protein 14-3-3, which recognizes two phosphoserines located in the linker between the caspase recruitment domain and the p19 domains of the caspase-2 zymogen. However, the structural details of this interaction and the exact role of 14-3-3 in the regulation of caspase-2 activation remain unclear. Moreover, the caspase-2 region with both 14-3-3-binding motifs also contains the nuclear localization sequence (NLS), thus suggesting that 14-3-3 binding may regulate the subcellular localization of caspase-2. Here, we report a structural analysis of the 14-3-3zeta:caspase-2 complex using a combined approach based on small angle X-ray scattering, NMR, chemical cross-linking, and fluorescence spectroscopy. The structural model proposed in this study suggests that phosphorylated caspase-2 and 14-3-3zeta form a compact and rigid complex in which the p19 and the p12 domains of caspase-2 are positioned within the central channel of the 14-3-3 dimer and stabilized through interactions with the C-terminal helices of both 14-3-3zeta protomers. In this conformation, the surface of the p12 domain, which is involved in caspase-2 activation by dimerization, is sterically occluded by the 14-3-3 dimer, thereby likely preventing caspase-2 activation. In addition, 14-3-3 protein binding to caspase-2 masks its NLS. Therefore, our results suggest that 14-3-3 protein binding to caspase-2 may play a key role in regulating caspase-2 activation. DATABASE: The atomic coordinates and structure factors have been deposited in the Protein Data Bank, www.ww pdb.org (PDB ID codes 6GKF and 6GKG).

~~Authors:~~ Alblova, M., Obsil, T., Obsilova, V.

14-3-3 protein masks the nuclear localization sequence of caspase-2.,Smidova A, Alblova M, Kalabova D, Psenakova K, Rosulek M, Herman P, Obsil T, Obsilova V FEBS J. 2018 Oct 3. doi: 10.1111/febs.14670. PMID:30281929<ref>PMID:30281929</ref>

~~Description~~: ~~Structure of~~ 14-3-3 ~~gamma in complex with caspase-2~~ 14-3-3 ~~binding motif Ser139~~

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

[[Category: ~~Unreleased~~ Structures]]

</div>

[[Category: ~~Obsil, T~~]]

[[Category: ~~Obsilova, V~~]]

[[Category: ~~Alblova, M~~]]

==See Also==

*[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]]

== References ==

__TOC__

</StructureSection>

[[Category: Homo sapiens]]

[[Category: Large Structures]]

[[Category: Alblova M]]

[[Category: Obsil T]]

[[Category: Obsilova V]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6gkf is ON HOLD  until Paper Publication
+==Structure of 14-3-3 gamma in complex with caspase-2 14-3-3 binding motif Ser139==
+<StructureSection load='6gkf' size='340' side='right'caption='[[6gkf]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6gkf]] is a 16 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=6GKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GKF FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.598&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=6gkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gkf OCA], [https://pdbe.org/6gkf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6gkf RCSB], [https://www.ebi.ac.uk/pdbsum/6gkf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6gkf ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/1433G_HUMAN 1433G_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.<ref>PMID:16511572</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Caspase-2 is an apical protease responsible for the proteolysis of cellular substrates directly involved in mediating apoptotic signaling cascades. Caspase-2 activation is inhibited by phosphorylation followed by binding to the scaffolding protein 14-3-3, which recognizes two phosphoserines located in the linker between the caspase recruitment domain and the p19 domains of the caspase-2 zymogen. However, the structural details of this interaction and the exact role of 14-3-3 in the regulation of caspase-2 activation remain unclear. Moreover, the caspase-2 region with both 14-3-3-binding motifs also contains the nuclear localization sequence (NLS), thus suggesting that 14-3-3 binding may regulate the subcellular localization of caspase-2. Here, we report a structural analysis of the 14-3-3zeta:caspase-2 complex using a combined approach based on small angle X-ray scattering, NMR, chemical cross-linking, and fluorescence spectroscopy. The structural model proposed in this study suggests that phosphorylated caspase-2 and 14-3-3zeta form a compact and rigid complex in which the p19 and the p12 domains of caspase-2 are positioned within the central channel of the 14-3-3 dimer and stabilized through interactions with the C-terminal helices of both 14-3-3zeta protomers. In this conformation, the surface of the p12 domain, which is involved in caspase-2 activation by dimerization, is sterically occluded by the 14-3-3 dimer, thereby likely preventing caspase-2 activation. In addition, 14-3-3 protein binding to caspase-2 masks its NLS. Therefore, our results suggest that 14-3-3 protein binding to caspase-2 may play a key role in regulating caspase-2 activation. DATABASE: The atomic coordinates and structure factors have been deposited in the Protein Data Bank, www.ww pdb.org (PDB ID codes 6GKF and 6GKG).
-Authors: Alblova, M., Obsil, T., Obsilova, V.
+-3-3 protein masks the nuclear localization sequence of caspase-2.,Smidova A, Alblova M, Kalabova D, Psenakova K, Rosulek M, Herman P, Obsil T, Obsilova V FEBS J. 2018 Oct 3. doi: 10.1111/febs.14670. PMID:30281929<ref>PMID:30281929</ref>
-Description: Structure of 14-3-3 gamma in complex with caspase-2 14-3-3 binding motif Ser139
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Obsil, T]]
+<div class="pdbe-citations 6gkf" style="background-color:#fffaf0;"></div>
-[[Category: Obsilova, V]]
-[[Category: Alblova, M]]
+==See Also==
+*[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Alblova M]]
+[[Category: Obsil T]]
+[[Category: Obsilova V]]