1xm2

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(New page: 200px<br /> <applet load="1xm2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xm2, resolution 2.7&Aring;" /> '''Crystal structure of...)
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[[Image:1xm2.gif|left|200px]]<br />
 
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<applet load="1xm2" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1xm2, resolution 2.7&Aring;" />
 
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'''Crystal structure of Human PRL-1'''<br />
 
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==Overview==
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==Crystal structure of Human PRL-1==
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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.
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<StructureSection load='1xm2' size='340' side='right'caption='[[1xm2]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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<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>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xm/1xm2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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1XM2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XM2 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15571731 15571731]
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</div>
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[[Category: Homo sapiens]]
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<div class="pdbe-citations 1xm2" style="background-color:#fffaf0;"></div>
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[[Category: Protein-tyrosine-phosphatase]]
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[[Category: Single protein]]
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[[Category: Jeong, D.G.]]
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[[Category: Kim, J.H.]]
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[[Category: Kim, S.J.]]
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[[Category: Ryu, S.E.]]
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[[Category: Son, J.H.]]
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[[Category: SO4]]
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[[Category: hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:07:32 2007''
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==See Also==
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*[[Dual specificity phosphatase 3D structures|Dual specificity phosphatase 3D structures]]
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*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Jeong DG]]
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[[Category: Kim JH]]
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[[Category: Kim SJ]]
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[[Category: Ryu SE]]
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[[Category: Son JH]]

Current revision

Crystal structure of Human PRL-1

PDB ID 1xm2

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