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| | <StructureSection load='2w10' size='340' side='right'caption='[[2w10]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='2w10' size='340' side='right'caption='[[2w10]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2w10]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W10 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2w10]] 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=2W10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W10 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2d0n|2d0n]], [[1r1q|1r1q]], [[1h3h|1h3h]], [[1r1s|1r1s]], [[1oeb|1oeb]], [[1uti|1uti]], [[1r1p|1r1p]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></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=2w10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w10 OCA], [https://pdbe.org/2w10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w10 RCSB], [https://www.ebi.ac.uk/pdbsum/2w10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w10 ProSAT]</span></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=2w10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w10 OCA], [https://pdbe.org/2w10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w10 RCSB], [https://www.ebi.ac.uk/pdbsum/2w10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w10 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PTN23_MOUSE PTN23_MOUSE]] May act as a negative regulator of Ras-mediated mitogenic activity. Plays a role in ciliogenesis.
| + | [https://www.uniprot.org/uniprot/GRAP2_MOUSE GRAP2_MOUSE] Interacts with SLP-76 to regulate NF-AT activation. Binds to tyrosine-phosphorylated shc. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Protein-tyrosine-phosphatase]]
| + | [[Category: Feller SM]] |
| - | [[Category: Feller, S M]] | + | [[Category: Harkiolaki M]] |
| - | [[Category: Harkiolaki, M]] | + | |
| - | [[Category: Alternative splicing]]
| + | |
| - | [[Category: Coiled coil]]
| + | |
| - | [[Category: Cytoplasm]]
| + | |
| - | [[Category: Cytoplasmic vesicle]]
| + | |
| - | [[Category: Dimer]]
| + | |
| - | [[Category: Gad]]
| + | |
| - | [[Category: Hd-ptp]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Mona]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Protein phosphatase]]
| + | |
| - | [[Category: Sh2 domain]]
| + | |
| - | [[Category: Sh3]]
| + | |
| - | [[Category: Sh3 domain]]
| + | |
| - | [[Category: Sh3 domain-complex]]
| + | |
| - | [[Category: Signal tranduction]]
| + | |
| - | [[Category: Tpr repeat]]
| + | |
| Structural highlights
Function
GRAP2_MOUSE Interacts with SLP-76 to regulate NF-AT activation. Binds to tyrosine-phosphorylated shc.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Grb2 and Gab2 form a complex implicated in normal cell signaling and cancer development. Binding of the Grb2SH3C domain to Gab2 is essential for the interaction, but molecular details remained undefined. Using peptide arrays and isothermal titration calorimetry, two Grb2SH3C binding sites in Gab2 (Gab2a and Gab2b) were confirmed and characterized. Gab2a bears similarity to a p27Kip1 epitope that also binds Grb2SH3C. Crystal structures of both Gab2 epitopes complexed with Grb2SH3C reveal that Gab2b contains a 3(10) helix that positions the arginine and lysine of the core-binding motif RxxK in parallel orientation. In contrast, the Gab2a RxxK motif is embedded in a PPII helix with Arg and Lys in staggered orientation. A similar interaction mode is also present in a new complex of Mona/GadsSH3C with an RxxxxK epitope from the putative phosphatase HD-PTP. In summary, our study reveals interaction types of SH3 domains, highlighting their great versatility.
Distinct binding modes of two epitopes in Gab2 that interact with the SH3C domain of Grb2.,Harkiolaki M, Tsirka T, Lewitzky M, Simister PC, Joshi D, Bird LE, Jones EY, O'Reilly N, Feller SM Structure. 2009 Jun 10;17(6):809-22. PMID:19523899[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Harkiolaki M, Tsirka T, Lewitzky M, Simister PC, Joshi D, Bird LE, Jones EY, O'Reilly N, Feller SM. Distinct binding modes of two epitopes in Gab2 that interact with the SH3C domain of Grb2. Structure. 2009 Jun 10;17(6):809-22. PMID:19523899 doi:10.1016/j.str.2009.03.017
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