We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2c23

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (14:02, 13 December 2023) (edit) (undo)
 
(13 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2c23.gif|left|200px]]
 
-
{{Structure
+
==14-3-3 Protein Beta (Human) in complex with exoenzyme S peptide==
-
|PDB= 2c23 |SIZE=350|CAPTION= <scene name='initialview01'>2c23</scene>, resolution 2.65&Aring;
+
<StructureSection load='2c23' size='340' side='right'caption='[[2c23]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND=
+
<table><tr><td colspan='2'>[[2c23]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C23 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C23 FirstGlance]. <br>
-
|ACTIVITY=
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65&#8491;</td></tr>
-
|GENE=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2c23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c23 OCA], [https://pdbe.org/2c23 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c23 RCSB], [https://www.ebi.ac.uk/pdbsum/2c23 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c23 ProSAT]</span></td></tr>
-
|DOMAIN=
+
</table>
-
|RELATEDENTRY=
+
== Function ==
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c23 OCA], [http://www.ebi.ac.uk/pdbsum/2c23 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c23 RCSB]</span>
+
[https://www.uniprot.org/uniprot/1433B_HUMAN 1433B_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. Negative regulator of osteogenesis. Blocks the nuclear translocation of the phosphorylated form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on cyclin D1 expression resulting in blockage of neuronal apoptosis elicited by SRPK2.<ref>PMID:17717073</ref> <ref>PMID:19592491</ref>
-
}}
+
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c2/2c23_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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=2c23 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The seven members of the human 14-3-3 protein family regulate a diverse range of cell signaling pathways by formation of protein-protein complexes with signaling proteins that contain phosphorylated Ser/Thr residues within specific sequence motifs. Previously, crystal structures of three 14-3-3 isoforms (zeta, sigma, and tau) have been reported, with structural data for two isoforms deposited in the Protein Data Bank (zeta and sigma). In this study, we provide structural detail for five 14-3-3 isoforms bound to ligands, providing structural coverage for all isoforms of a human protein family. A comparative structural analysis of the seven 14-3-3 proteins revealed specificity determinants for binding of phosphopeptides in a specific orientation, target domain interaction surfaces and flexible adaptation of 14-3-3 proteins through domain movements. Specifically, the structures of the beta isoform in its apo and peptide bound forms showed that its binding site can exhibit structural flexibility to facilitate binding of its protein and peptide partners. In addition, the complex of 14-3-3 beta with the exoenzyme S peptide displayed a secondary structural element in the 14-3-3 peptide binding groove. These results show that the 14-3-3 proteins are adaptable structures in which internal flexibility is likely to facilitate recognition and binding of their interaction partners.
-
'''14-3-3 PROTEIN BETA (HUMAN) IN COMPLEX WITH EXOENZYME S PEPTIDE'''
+
Structural basis for protein-protein interactions in the 14-3-3 protein family.,Yang X, Lee WH, Sobott F, Papagrigoriou E, Robinson CV, Grossmann JG, Sundstrom M, Doyle DA, Elkins JM Proc Natl Acad Sci U S A. 2006 Nov 14;103(46):17237-42. Epub 2006 Nov 3. PMID:17085597<ref>PMID:17085597</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 2c23" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
The seven members of the human 14-3-3 protein family regulate a diverse range of cell signaling pathways by formation of protein-protein complexes with signaling proteins that contain phosphorylated Ser/Thr residues within specific sequence motifs. Previously, crystal structures of three 14-3-3 isoforms (zeta, sigma, and tau) have been reported, with structural data for two isoforms deposited in the Protein Data Bank (zeta and sigma). In this study, we provide structural detail for five 14-3-3 isoforms bound to ligands, providing structural coverage for all isoforms of a human protein family. A comparative structural analysis of the seven 14-3-3 proteins revealed specificity determinants for binding of phosphopeptides in a specific orientation, target domain interaction surfaces and flexible adaptation of 14-3-3 proteins through domain movements. Specifically, the structures of the beta isoform in its apo and peptide bound forms showed that its binding site can exhibit structural flexibility to facilitate binding of its protein and peptide partners. In addition, the complex of 14-3-3 beta with the exoenzyme S peptide displayed a secondary structural element in the 14-3-3 peptide binding groove. These results show that the 14-3-3 proteins are adaptable structures in which internal flexibility is likely to facilitate recognition and binding of their interaction partners.
+
*[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
2C23 is a [[Protein complex]] structure of sequences 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=2C23 OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
-
Structural basis for protein-protein interactions in the 14-3-3 protein family., Yang X, Lee WH, Sobott F, Papagrigoriou E, Robinson CV, Grossmann JG, Sundstrom M, Doyle DA, Elkins JM, Proc Natl Acad Sci U S A. 2006 Nov 14;103(46):17237-42. Epub 2006 Nov 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17085597 17085597]
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Protein complex]]
+
[[Category: Large Structures]]
-
[[Category: Arrowsmith, C.]]
+
[[Category: Pseudomonas aeruginosa]]
-
[[Category: Doyle, D A.]]
+
[[Category: Arrowsmith C]]
-
[[Category: Edwards, A.]]
+
[[Category: Doyle DA]]
-
[[Category: Elkins, J M.]]
+
[[Category: Edwards A]]
-
[[Category: Schoch, G A.]]
+
[[Category: Elkins JM]]
-
[[Category: Sundstrom, M.]]
+
[[Category: Schoch GA]]
-
[[Category: Yang, X.]]
+
[[Category: Sundstrom M]]
-
[[Category: 14-3-3,ywhab,exos,exoenzyme s,structural genomic]]
+
[[Category: Yang X]]
-
[[Category: structural genomics consortium,acetylation,alternative initiation,phosphorylation,cell regulator protein]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:15:09 2008''
+

Current revision

14-3-3 Protein Beta (Human) in complex with exoenzyme S peptide

PDB ID 2c23

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2c23"
Personal tools