5wfu
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5wfu is ON HOLD until Jul 12 2019 Authors: Hou, Z.Q., Liu, X.Y. Description: Structural basis for the interaction of 14-3-3beta with Tricarboxylic ...) |
|||
| (3 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Structural basis for the interaction of 14-3-3beta with Tricarboxylic Acid Cycle intermediate Malate== | |
| + | <StructureSection load='5wfu' size='340' side='right'caption='[[5wfu]], [[Resolution|resolution]] 1.97Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5wfu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WFU 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]] 1.97Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLT:D-MALATE'>MLT</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=5wfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wfu OCA], [https://pdbe.org/5wfu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wfu RCSB], [https://www.ebi.ac.uk/pdbsum/5wfu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wfu ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/1433B_MOUSE 1433B_MOUSE] 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 (By similarity). | ||
| - | + | ==See Also== | |
| - | + | *[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]] | |
| - | + | __TOC__ | |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Hou | + | [[Category: Mus musculus]] |
| + | [[Category: Hou ZQ]] | ||
| + | [[Category: Liu XY]] | ||
Current revision
Structural basis for the interaction of 14-3-3beta with Tricarboxylic Acid Cycle intermediate Malate
| |||||||||||
