1x24: Difference between revisions

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-{{Seed}}
-[[Image:1x24.png|left|200px]]
-<!--
+==Prl-1 (ptp4a)==
-The line below this paragraph, containing "STRUCTURE_1x24", creates the "Structure Box" on the page.
+<StructureSection load='1x24' size='340' side='right'caption='[[1x24]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1x24]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X24 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X24 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</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=1x24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x24 OCA], [https://pdbe.org/1x24 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x24 RCSB], [https://www.ebi.ac.uk/pdbsum/1x24 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x24 ProSAT]</span></td></tr>
-{{STRUCTURE_1x24|  PDB=1x24  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TP4A1_RAT TP4A1_RAT] 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 (By similarity).
+== 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/x2/1x24_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=1x24 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The PRL (phosphatase of regenerating liver) phosphatases constitute a novel class of small, prenylated phosphatases that are implicated in promoting cell growth, differentiation, and tumor invasion, and represent attractive targets for anticancer therapy. Here we describe the crystal structures of native PRL-1 as well as the catalytically inactive mutant PRL-1/C104S in complex with sulfate. PRL-1 exists as a trimer in the crystalline state, burying 1140 A2 of accessible surface area at each dimer interface. Trimerization creates a large, bipartite membrane-binding surface in which the exposed C-terminal basic residues could cooperate with the adjacent prenylation group to anchor PRL-1 on the acidic inner membrane. Structural and kinetic analyses place PRL-1 in the family of dual specificity phopsphatases with closest structural similarity to the Cdc14 phosphatase and provide a molecular basis for catalytic activation of the PRL phosphatases. Finally, native PRL-1 is crystallized in an oxidized form in which a disulfide is formed between the active site Cys104 and a neighboring residue Cys49, which blocks both substrate binding and catalysis. Biochemical studies in solution and in the cell support a potential regulatory role of this intramolecular disulfide bond formation in response to reactive oxygen species such as H2O2.
-===Prl-1 (ptp4a)===
+Structure and biochemical properties of PRL-1, a phosphatase implicated in cell growth, differentiation, and tumor invasion.,Sun JP, Wang WQ, Yang H, Liu S, Liang F, Fedorov AA, Almo SC, Zhang ZY Biochemistry. 2005 Sep 13;44(36):12009-21. PMID:16142898<ref>PMID:16142898</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1x24" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_16142898}}, adds the Publication Abstract to the page
+*[[Dual specificity phosphatase 3D structures|Dual specificity phosphatase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 16142898 is the PubMed ID number.
+*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
--->
+== References ==
-{{ABSTRACT_PUBMED_16142898}}
+<references/>
+__TOC__
-==About this Structure==
+</StructureSection>
-X24 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X24 OCA].
+[[Category: Large Structures]]
-==Reference==
-Structure and biochemical properties of PRL-1, a phosphatase implicated in cell growth, differentiation, and tumor invasion., Sun JP, Wang WQ, Yang H, Liu S, Liang F, Fedorov AA, Almo SC, Zhang ZY, Biochemistry. 2005 Sep 13;44(36):12009-21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16142898 16142898]
-[[Category: Protein-tyrosine-phosphatase]]
 [[Category: Rattus norvegicus]]
-[[Category: Single protein]]
+[[Category: Liu S]]
-[[Category: Liu, S.]]
+[[Category: Sun JP]]
-[[Category: Sun, J P.]]
+[[Category: Wang WQ]]
-[[Category: Wang, W Q.]]
+[[Category: Yang H]]
-[[Category: Yang, H.]]
+[[Category: Zhang ZY]]
-[[Category: Zhang, Z Y.]]
-[[Category: Dual specific phosphatase]]
-[[Category: Prl-1]]
-[[Category: Tyrosine phosphatase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:26:30 2008''