1xm2: Difference between revisions

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-[[Image:1xm2.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1xm2", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
--->
-{{STRUCTURE_1xm2|  PDB=1xm2  |  SCENE=  }}
-'''Crystal structure of Human PRL-1'''
+==Crystal structure of Human PRL-1==
+<StructureSection load='1xm2' size='340' side='right'caption='[[1xm2]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1xm2]] is a 6 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=1XM2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XM2 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]] 2.7&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1xm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xm2 OCA], [https://pdbe.org/1xm2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xm2 RCSB], [https://www.ebi.ac.uk/pdbsum/1xm2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xm2 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TP4A1_HUMAN TP4A1_HUMAN] Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. May play a role in the development and maintenance of differentiating epithelial tissues. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis.<ref>PMID:12235145</ref> <ref>PMID:14643450</ref> <ref>PMID:12782572</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xm/1xm2_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xm2 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The PRL phosphatases, which constitute a subfamily of the protein tyrosine phosphatases (PTPs), are implicated in oncogenic and metastatic processes. Here, we report the crystal structure of human PRL-1 determined at 2.7A resolution. The crystal structure reveals the shallow active-site pocket with highly hydrophobic character. A structural comparison with the previously determined NMR structure of PRL-3 exhibits significant differences in the active-site region. In the PRL-1 structure, a sulfate ion is bound to the active-site, providing stabilizing interactions to maintain the canonically found active conformation of PTPs, whereas the NMR structure exhibits an open conformation of the active-site. We also found that PRL-1 forms a trimer in the crystal and the trimer exists in the membrane fraction of cells, suggesting the possible biological regulation of PRL-1 activity by oligomerization. The detailed structural information on the active enzyme conformation and regulation of PRL-1 provides the structural basis for the development of potential inhibitors of PRL enzymes.
-==Overview==
+Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms.,Jeong DG, Kim SJ, Kim JH, Son JH, Park MR, Lim SM, Yoon TS, Ryu SE J Mol Biol. 2005 Jan 14;345(2):401-13. PMID:15571731<ref>PMID:15571731</ref>
-The PRL phosphatases, which constitute a subfamily of the protein tyrosine phosphatases (PTPs), are implicated in oncogenic and metastatic processes. Here, we report the crystal structure of human PRL-1 determined at 2.7A resolution. The crystal structure reveals the shallow active-site pocket with highly hydrophobic character. A structural comparison with the previously determined NMR structure of PRL-3 exhibits significant differences in the active-site region. In the PRL-1 structure, a sulfate ion is bound to the active-site, providing stabilizing interactions to maintain the canonically found active conformation of PTPs, whereas the NMR structure exhibits an open conformation of the active-site. We also found that PRL-1 forms a trimer in the crystal and the trimer exists in the membrane fraction of cells, suggesting the possible biological regulation of PRL-1 activity by oligomerization. The detailed structural information on the active enzyme conformation and regulation of PRL-1 provides the structural basis for the development of potential inhibitors of PRL enzymes.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-XM2 is a [[Single protein]] structure of 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=1XM2 OCA].
+</div>
+<div class="pdbe-citations 1xm2" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms., Jeong DG, Kim SJ, Kim JH, Son JH, Park MR, Lim SM, Yoon TS, Ryu SE, J Mol Biol. 2005 Jan 14;345(2):401-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15571731 15571731]
+*[[Dual specificity phosphatase 3D structures|Dual specificity phosphatase 3D structures]]
+*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Protein-tyrosine-phosphatase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Jeong DG]]
-[[Category: Jeong, D G.]]
+[[Category: Kim JH]]
-[[Category: Kim, J H.]]
+[[Category: Kim SJ]]
-[[Category: Kim, S J.]]
+[[Category: Ryu SE]]
-[[Category: Ryu, S E.]]
+[[Category: Son JH]]
-[[Category: Son, J H.]]
-[[Category: Hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 15:12:16 2008''