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| | ==Crystal structure of the complex between human PRL-2 phosphatase in reduced state and Bateman domain of human CNNM3== | | ==Crystal structure of the complex between human PRL-2 phosphatase in reduced state and Bateman domain of human CNNM3== |
| - | <StructureSection load='5k22' size='340' side='right' caption='[[5k22]], [[Resolution|resolution]] 3.00Å' scene=''> | + | <StructureSection load='5k22' size='340' side='right'caption='[[5k22]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5k22]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K22 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5k22]] 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=5K22 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K22 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5k23|5k23]], [[5k24|5k24]], [[5k25|5k25]]</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]] 3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PTP4A2, PRL2, PTPCAAX2, BM-008 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CNNM3, ACDP3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5k22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k22 OCA], [https://pdbe.org/5k22 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k22 RCSB], [https://www.ebi.ac.uk/pdbsum/5k22 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k22 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5k22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k22 OCA], [http://pdbe.org/5k22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k22 RCSB], [http://www.ebi.ac.uk/pdbsum/5k22 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k22 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TP4A2_HUMAN TP4A2_HUMAN]] Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Promotes tumors. Inhibits geranylgeranyl transferase type II activity by blocking the association between RABGGTA and RABGGTB.<ref>PMID:14643450</ref> [[http://www.uniprot.org/uniprot/CNNM3_HUMAN CNNM3_HUMAN]] Probable metal transporter. | + | [https://www.uniprot.org/uniprot/CNNM3_HUMAN CNNM3_HUMAN] Probable metal transporter. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Tyrosine phosphatase|Tyrosine phosphatase]] | + | *[[Dual specificity phosphatase 3D structures|Dual specificity phosphatase 3D structures]] |
| | + | *[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Protein-tyrosine-phosphatase]] | + | [[Category: Large Structures]] |
| - | [[Category: Gehring, K]] | + | [[Category: Gehring K]] |
| - | [[Category: Kozlov, G]] | + | [[Category: Kozlov G]] |
| - | [[Category: Wu, H]] | + | [[Category: Wu H]] |
| - | [[Category: Alpha-beta fold]]
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| - | [[Category: Complex]]
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| - | [[Category: Phosphatase]]
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| - | [[Category: Protein binding]]
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| - | [[Category: Transport protein-protein binding complex]]
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| Structural highlights
Function
CNNM3_HUMAN Probable metal transporter.
Publication Abstract from PubMed
PRLs (phosphatases of regenerating liver) are frequently overexpressed in human cancers and are prognostic markers of poor survival. Despite their potential as therapeutic targets, their mechanism of action is not understood in part due to their weak enzymatic activity. Previous studies revealed that PRLs interact with CNNM ion transporters and prevent CNNM4-dependent Mg(2+) transport, which is important for energy metabolism and tumor progression. Here, we report that PRL-CNNM complex formation is regulated by the formation of phosphocysteine. We show that cysteine in the PRL catalytic site is endogenously phosphorylated as part of the catalytic cycle and that phosphocysteine levels change in response to Mg(2+) levels. Phosphorylation blocks PRL binding to CNNM Mg(2+) transporters, and mutations that block the PRL-CNNM interaction prevent regulation of Mg(2+) efflux in cultured cells. The crystal structure of the complex of PRL2 and the CBS-pair domain of the Mg(2+) transporter CNNM3 reveals the molecular basis for the interaction. The identification of phosphocysteine as a regulatory modification opens new perspectives for signaling by protein phosphatases.
Phosphocysteine in the PRL-CNNM pathway mediates magnesium homeostasis.,Gulerez I, Funato Y, Wu H, Yang M, Kozlov G, Miki H, Gehring K EMBO Rep. 2016 Dec;17(12):1890-1900. doi: 10.15252/embr.201643393. Epub 2016 Nov , 17. PMID:27856537[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gulerez I, Funato Y, Wu H, Yang M, Kozlov G, Miki H, Gehring K. Phosphocysteine in the PRL-CNNM pathway mediates magnesium homeostasis. EMBO Rep. 2016 Dec;17(12):1890-1900. doi: 10.15252/embr.201643393. Epub 2016 Nov , 17. PMID:27856537 doi:http://dx.doi.org/10.15252/embr.201643393
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