3ux0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:32, 6 November 2024) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Crystal structure of human 14-3-3 sigma in complex with TASK-3 peptide and stabilizer Fusicoccin H==
==Crystal structure of human 14-3-3 sigma in complex with TASK-3 peptide and stabilizer Fusicoccin H==
-
<StructureSection load='3ux0' size='340' side='right' caption='[[3ux0]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
+
<StructureSection load='3ux0' size='340' side='right'caption='[[3ux0]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3ux0]] is a 2 chain structure with 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=3UX0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UX0 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3ux0]] 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=3UX0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UX0 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0DV:(4R,5R,6R,6AS,9S,9AE,10AR)-5-HYDROXY-9-(HYDROXYMETHYL)-6,10A-DIMETHYL-3-(PROPAN-2-YL)-1,2,4,5,6,6A,7,8,9,10A-DECAHYDRODICYCLOPENTA[A,D][8]ANNULEN-4-YL+ALPHA-D-GULOPYRANOSIDE'>0DV</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.75&#8491;</td></tr>
-
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <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=0DV:(4R,5R,6R,6AS,9S,9AE,10AR)-5-HYDROXY-9-(HYDROXYMETHYL)-6,10A-DIMETHYL-3-(PROPAN-2-YL)-1,2,4,5,6,6A,7,8,9,10A-DECAHYDRODICYCLOPENTA[A,D][8]ANNULEN-4-YL+ALPHA-D-GULOPYRANOSIDE'>0DV</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3p1n|3p1n]], [[3p1o|3p1o]], [[3p1p|3p1p]], [[3p1q|3p1q]], [[3p1r|3p1r]], [[3p1s|3p1s]]</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=3ux0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ux0 OCA], [https://pdbe.org/3ux0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ux0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ux0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ux0 ProSAT]</span></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HME1, SFN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3ux0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ux0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ux0 RCSB], [http://www.ebi.ac.uk/pdbsum/3ux0 PDBsum]</span></td></tr>
+
</table>
</table>
-
== Disease ==
 
-
[[http://www.uniprot.org/uniprot/KCNK9_HUMAN KCNK9_HUMAN]] Intellectual deficit, Birk-Barel type. Birk-Barel mental retardation dysmorphism syndrome (BIBAS) [MIM:[http://omim.org/entry/612292 612292]]: A syndrome characterized by mental retardation, hypotonia, hyperactivity, and facial dysmorphism. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:18678320</ref>
 
== Function ==
== 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. [[http://www.uniprot.org/uniprot/KCNK9_HUMAN KCNK9_HUMAN]] pH-dependent, voltage-insensitive, background potassium channel protein.<ref>PMID:11042359</ref> <ref>PMID:11431495</ref>
+
[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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 21: Line 18:
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
 +
<div class="pdbe-citations 3ux0" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
-
*[[14-3-3 protein|14-3-3 protein]]
+
*[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
Line 29: Line 27:
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Anders, C]]
+
[[Category: Large Structures]]
-
[[Category: Bartel, M]]
+
[[Category: Anders C]]
-
[[Category: Higuchi, Y]]
+
[[Category: Bartel M]]
-
[[Category: Kato, N]]
+
[[Category: Higuchi Y]]
-
[[Category: Ottmann, C]]
+
[[Category: Kato N]]
-
[[Category: Schumacher, B]]
+
[[Category: Ottmann C]]
-
[[Category: Thiel, P]]
+
[[Category: Schumacher B]]
-
[[Category: Adapter protein]]
+
[[Category: Thiel P]]
-
[[Category: Helical protein]]
+
-
[[Category: Nucleus]]
+
-
[[Category: Peptide binding protein]]
+
-
[[Category: Phosphoprotein]]
+

Current revision

Crystal structure of human 14-3-3 sigma in complex with TASK-3 peptide and stabilizer Fusicoccin H

PDB ID 3ux0

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools