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| | ==Structure of VHZ bound to metavanadate== | | ==Structure of VHZ bound to metavanadate== |
| - | <StructureSection load='4erc' size='340' side='right' caption='[[4erc]], [[Resolution|resolution]] 1.15Å' scene=''> | + | <StructureSection load='4erc' size='340' side='right'caption='[[4erc]], [[Resolution|resolution]] 1.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4erc]] 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=4ERC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ERC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4erc]] 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=4ERC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ERC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=VN4:OXIDO(DIOXO)VANADIUM'>VN4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=VN4:OXIDO(DIOXO)VANADIUM'>VN4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2img|2img]]</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=4erc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4erc OCA], [https://pdbe.org/4erc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4erc RCSB], [https://www.ebi.ac.uk/pdbsum/4erc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4erc ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DUSP23, LDP3, VHZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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| - | <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=4erc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4erc OCA], [http://pdbe.org/4erc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4erc RCSB], [http://www.ebi.ac.uk/pdbsum/4erc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4erc ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DUS23_HUMAN DUS23_HUMAN]] Protein phosphatase that mediates dephosphorylation of proteins phosphorylated on Tyr and Ser/Thr residues. In vitro, it can dephosphorylate p44-ERK1 (MAPK3) but not p54 SAPK-beta (MAPK10) in vitro. Able to enhance activation of JNK and p38 (MAPK14).<ref>PMID:15201283</ref> <ref>PMID:15147733</ref> | + | [https://www.uniprot.org/uniprot/DUS23_HUMAN DUS23_HUMAN] Protein phosphatase that mediates dephosphorylation of proteins phosphorylated on Tyr and Ser/Thr residues. In vitro, it can dephosphorylate p44-ERK1 (MAPK3) but not p54 SAPK-beta (MAPK10) in vitro. Able to enhance activation of JNK and p38 (MAPK14).<ref>PMID:15201283</ref> <ref>PMID:15147733</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4erc" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4erc" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Dual specificity phosphatase 3D structures|Dual specificity phosphatase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Alvan, C H]] | + | [[Category: Large Structures]] |
| - | [[Category: Sean, J J]] | + | [[Category: Alvan CH]] |
| - | [[Category: Vyacheslav, K]] | + | [[Category: Sean JJ]] |
| - | [[Category: Alpha beta]] | + | [[Category: Vyacheslav K]] |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
DUS23_HUMAN Protein phosphatase that mediates dephosphorylation of proteins phosphorylated on Tyr and Ser/Thr residues. In vitro, it can dephosphorylate p44-ERK1 (MAPK3) but not p54 SAPK-beta (MAPK10) in vitro. Able to enhance activation of JNK and p38 (MAPK14).[1] [2]
Publication Abstract from PubMed
The recently discovered 150-residue human VHZ (VH1-related protein, Z member) is one of the smallest protein tyrosine phosphatases (PTPs) known and contains only the minimal structural elements common to all PTPs. We report a substrate screening analysis and a crystal structure of the VHZ complex with vanadate at 1.1 A resolution, with a detailed structural comparison with other members of the protein tyrosine phosphatase family, including classical tyrosine-specific protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DSPs). A screen with 360 phosphorylated peptides shows VHZ efficiently catalyzes the hydrolysis of phosphotyrosine (pY)-containing peptides but exhibits no activity toward phosphoserine (pS) or phosphothreonine (pT) peptides. The new structure reveals a deep and narrow active site more typical of the classical tyrosine-specific PTPs. Despite the high degrees of structural and sequence similarity between VHZ and classical PTPs, its general acid IPD-loop is most likely conformationally rigid, in contrast to the flexible WPD counterpart of classical PTPs. VHZ also lacks substrate recognition domains and other domains typically found on classical PTPs. It is therefore proposed that VHZ is more properly classified as an atypical PTP rather than an atypical DSP, as has been suggested.
New Aspects of the Phosphatase VHZ Revealed by a High-Resolution Structure with Vanadate and Substrate Screening.,Kuznetsov VI, Hengge AC, Johnson SJ Biochemistry. 2012 Nov 26. PMID:23145819[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Alonso A, Burkhalter S, Sasin J, Tautz L, Bogetz J, Huynh H, Bremer MC, Holsinger LJ, Godzik A, Mustelin T. The minimal essential core of a cysteine-based protein-tyrosine phosphatase revealed by a novel 16-kDa VH1-like phosphatase, VHZ. J Biol Chem. 2004 Aug 20;279(34):35768-74. Epub 2004 Jun 16. PMID:15201283 doi:http://dx.doi.org/10.1074/jbc.M403412200
- ↑ Wu Q, Li Y, Gu S, Li N, Zheng D, Li D, Zheng Z, Ji C, Xie Y, Mao Y. Molecular cloning and characterization of a novel dual-specificity phosphatase 23 gene from human fetal brain. Int J Biochem Cell Biol. 2004 Aug;36(8):1542-53. PMID:15147733 doi:http://dx.doi.org/10.1016/j.biocel.2003.12.014
- ↑ Kuznetsov VI, Hengge AC, Johnson SJ. New Aspects of the Phosphatase VHZ Revealed by a High-Resolution Structure with Vanadate and Substrate Screening. Biochemistry. 2012 Nov 26. PMID:23145819 doi:http://dx.doi.org/10.1021/bi300908y
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