2b05: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
(11 intermediate revisions by the same user not shown) | |||
Line 1: | Line 1: | ||
==Crystal Structure of 14-3-3 gamma in complex with a phosphoserine peptide== | |||
<StructureSection load='2b05' size='340' side='right'caption='[[2b05]], [[Resolution|resolution]] 2.55Å' scene=''> | |||
| | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2b05]] is a 12 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=2B05 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B05 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]] 2.55Å</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=2b05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b05 OCA], [https://pdbe.org/2b05 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b05 RCSB], [https://www.ebi.ac.uk/pdbsum/2b05 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b05 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> | |||
== 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/b0/2b05_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2b05 ConSurf]. | |||
<div style="clear:both"></div> | |||
==See Also== | |||
*[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]] | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Arrowsmith | [[Category: Arrowsmith C]] | ||
[[Category: Debreczeni | [[Category: Debreczeni EJ]] | ||
[[Category: Doyle D]] | |||
[[Category: Doyle | [[Category: Edwards A]] | ||
[[Category: Edwards | [[Category: Elkins J]] | ||
[[Category: Elkins | [[Category: Papagrigoriou E]] | ||
[[Category: Papagrigoriou | [[Category: Turnbull A]] | ||
[[Category: Turnbull | [[Category: Weigelt J]] | ||
[[Category: Weigelt | [[Category: Yang X]] | ||
[[Category: Yang | [[Category: Zhao Y]] | ||
[[Category: Zhao | [[Category: Von Delft F]] | ||
[[Category: | |||
Latest revision as of 12:00, 6 November 2024
Crystal Structure of 14-3-3 gamma in complex with a phosphoserine peptideCrystal Structure of 14-3-3 gamma in complex with a phosphoserine peptide
Structural highlights
Function1433G_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.[1] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See AlsoReferences
|
|