1yz5

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{{Seed}}
 
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[[Image:1yz5.png|left|200px]]
 
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==The crystal structure of 14-3-3-sigma at 2.8 angstrom resolution==
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The line below this paragraph, containing "STRUCTURE_1yz5", creates the "Structure Box" on the page.
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<StructureSection load='1yz5' size='340' side='right'caption='[[1yz5]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1yz5]] is a 2 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=1YZ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YZ5 FirstGlance]. <br>
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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]] 2.8&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yz5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yz5 OCA], [https://pdbe.org/1yz5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yz5 RCSB], [https://www.ebi.ac.uk/pdbsum/1yz5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yz5 ProSAT]</span></td></tr>
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{{STRUCTURE_1yz5| PDB=1yz5 | SCENE= }}
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yz/1yz5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1yz5 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Seven different, but highly conserved 14-3-3 proteins are involved in diverse signaling pathways in human cells. It is unclear how the 14-3-3sigma isoform, a transcriptional target of p53, exerts its inhibitory effect on the cell cycle in the presence of other 14-3-3 isoforms, which are constitutively expressed at high levels. In order to identify structural differences between the 14-3-3 isoforms, we solved the crystal structure of the human 14-3-3sigma protein at a resolution of 2.8 Angstroms and compared it to the known structures of 14-3-3zeta and 14-3-3tau. The global architecture of the 14-3-3sigma fold is similar to the previously determined structures of 14-3-3zeta and 14-3-3t: two 14-3-3sigma molecules form a cup-shaped dimer. Significant differences between these 14-3-3 isoforms were detected adjacent to the amphipathic groove, which mediates the binding to phosphorylated consensus motifs in 14-3-3-ligands. Another specificity determining region is localized between amino-acids 203 to 215. These differences presumably select for the interaction with specific ligands, which may explain the different biological functions of the respective 14-3-3 isoforms. Furthermore, the two 14-3-3sigma molecules forming a dimer differ by the spatial position of the ninth helix, which is shifted to the inside of the ligand interaction surface, thus indicating adaptability of this part of the molecule. In addition, 5 non-conserved residues are located at the interface between two 14-3-3sigma proteins forming a dimer and represent candidate determinants of homo- and hetero-dimerization specificity. The structural differences among the 14-3-3 isoforms described here presumably contribute to isoform-specific interactions and functions.
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===The crystal structure of 14-3-3-sigma at 2.8 angstrom resolution===
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The crystal structure of the non-liganded 14-3-3sigma protein: insights into determinants of isoform specific ligand binding and dimerization.,Benzinger A, Popowicz GM, Joy JK, Majumdar S, Holak TA, Hermeking H Cell Res. 2005 Apr;15(4):219-27. PMID:15857576<ref>PMID:15857576</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 1yz5" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15857576}}, adds the Publication Abstract to the page
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*[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 15857576 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15857576}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1YZ5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YZ5 OCA].
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==Reference==
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The crystal structure of the non-liganded 14-3-3sigma protein: insights into determinants of isoform specific ligand binding and dimerization., Benzinger A, Popowicz GM, Joy JK, Majumdar S, Holak TA, Hermeking H, Cell Res. 2005 Apr;15(4):219-27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15857576 15857576]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Benzinger, A.]]
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[[Category: Benzinger A]]
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[[Category: Hermeking, H.]]
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[[Category: Hermeking H]]
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[[Category: Holak, T A.]]
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[[Category: Holak TA]]
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[[Category: Popowicz, G M.]]
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[[Category: Popowicz GM]]
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[[Category: Helix bundle]]
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[[Category: Homodimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:27:45 2008''
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Current revision

The crystal structure of 14-3-3-sigma at 2.8 angstrom resolution

PDB ID 1yz5

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