2gjt

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of the human receptor phosphatase PTPRO

Structural highlights

2gjt is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.15Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

PTPRO_HUMAN Defects in PTPRO are the cause of nephrotic syndrome type 6 (NPHS6) [MIM:614196. NPHS6 is a renal disease characterized clinically by proteinuria, hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form and progress to end-stage renal failure.^[1]

Function

PTPRO_HUMAN Possesses tyrosine phosphatase activity. Plays a role in regulating the glomerular pressure/filtration rate relationship through an effect on podocyte structure and function (By similarity).^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Protein tyrosine phosphatases (PTPs) play a critical role in regulating cellular functions by selectively dephosphorylating their substrates. Here we present 22 human PTP crystal structures that, together with prior structural knowledge, enable a comprehensive analysis of the classical PTP family. Despite their largely conserved fold, surface properties of PTPs are strikingly diverse. A potential secondary substrate-binding pocket is frequently found in phosphatases, and this has implications for both substrate recognition and development of selective inhibitors. Structural comparison identified four diverse catalytic loop (WPD) conformations and suggested a mechanism for loop closure. Enzymatic assays revealed vast differences in PTP catalytic activity and identified PTPD1, PTPD2, and HDPTP as catalytically inert protein phosphatases. We propose a "head-to-toe" dimerization model for RPTPgamma/zeta that is distinct from the "inhibitory wedge" model and that provides a molecular basis for inhibitory regulation. This phosphatome resource gives an expanded insight into intrafamily PTP diversity, catalytic activity, substrate recognition, and autoregulatory self-association.

Large-scale structural analysis of the classical human protein tyrosine phosphatome.,Barr AJ, Ugochukwu E, Lee WH, King ON, Filippakopoulos P, Alfano I, Savitsky P, Burgess-Brown NA, Muller S, Knapp S Cell. 2009 Jan 23;136(2):352-63. PMID:19167335^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ozaltin F, Ibsirlioglu T, Taskiran EZ, Baydar DE, Kaymaz F, Buyukcelik M, Kilic BD, Balat A, Iatropoulos P, Asan E, Akarsu NA, Schaefer F, Yilmaz E, Bakkaloglu A. Disruption of PTPRO causes childhood-onset nephrotic syndrome. Am J Hum Genet. 2011 Jul 15;89(1):139-47. doi: 10.1016/j.ajhg.2011.05.026. Epub, 2011 Jun 30. PMID:21722858 doi:10.1016/j.ajhg.2011.05.026
↑ Barr AJ, Ugochukwu E, Lee WH, King ON, Filippakopoulos P, Alfano I, Savitsky P, Burgess-Brown NA, Muller S, Knapp S. Large-scale structural analysis of the classical human protein tyrosine phosphatome. Cell. 2009 Jan 23;136(2):352-63. PMID:19167335 doi:http://dx.doi.org/10.1016/j.cell.2008.11.038
↑ Barr AJ, Ugochukwu E, Lee WH, King ON, Filippakopoulos P, Alfano I, Savitsky P, Burgess-Brown NA, Muller S, Knapp S. Large-scale structural analysis of the classical human protein tyrosine phosphatome. Cell. 2009 Jan 23;136(2):352-63. PMID:19167335 doi:http://dx.doi.org/10.1016/j.cell.2008.11.038

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 See Also
7 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2gjt"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the human receptor phosphatase PTPRO==
-<StructureSection load='2gjt' size='340' side='right' caption='[[2gjt]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
+<StructureSection load='2gjt' size='340' side='right'caption='[[2gjt]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2gjt]] is a 2 chain structure with 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=2GJT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GJT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2gjt]] 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=2GJT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GJT FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene><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]] 2.15&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ahs|2ahs]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
-<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PTPRO, GLEPP1, PTPU2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=2gjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gjt OCA], [https://pdbe.org/2gjt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gjt RCSB], [https://www.ebi.ac.uk/pdbsum/2gjt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gjt ProSAT]</span></td></tr>
-<tr><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>
+</table>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gjt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2gjt RCSB], [http://www.ebi.ac.uk/pdbsum/2gjt PDBsum]</span></td></tr>
-<table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/PTPRO_HUMAN PTPRO_HUMAN]] Defects in PTPRO are the cause of nephrotic syndrome type 6 (NPHS6) [MIM:[http://omim.org/entry/614196 614196]]. NPHS6 is a renal disease characterized clinically by proteinuria, hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form and progress to end-stage renal failure.<ref>PMID:21722858</ref>
+[https://www.uniprot.org/uniprot/PTPRO_HUMAN PTPRO_HUMAN] Defects in PTPRO are the cause of nephrotic syndrome type 6 (NPHS6) [MIM:[https://omim.org/entry/614196 614196]. NPHS6 is a renal disease characterized clinically by proteinuria, hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form and progress to end-stage renal failure.<ref>PMID:21722858</ref>
 == Function ==
-[[http://www.uniprot.org/uniprot/PTPRO_HUMAN PTPRO_HUMAN]] Possesses tyrosine phosphatase activity. Plays a role in regulating the glomerular pressure/filtration rate relationship through an effect on podocyte structure and function (By similarity).<ref>PMID:19167335</ref>
+[https://www.uniprot.org/uniprot/PTPRO_HUMAN PTPRO_HUMAN] Possesses tyrosine phosphatase activity. Plays a role in regulating the glomerular pressure/filtration rate relationship through an effect on podocyte structure and function (By similarity).<ref>PMID:19167335</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/gj/2gjt_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gj/2gjt_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=2gjt ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 31: / Line 30: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2gjt" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Tyrosine phosphatase|Tyrosine phosphatase]]
+*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
 == References ==
 <references/>
@@ Line 39: / Line 39: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Protein-tyrosine-phosphatase]]
+[[Category: Large Structures]]
-[[Category: Arrowsmith, C.]]
+[[Category: Arrowsmith C]]
-[[Category: Barr, A.]]
+[[Category: Barr A]]
-[[Category: Das, S.]]
+[[Category: Das S]]
-[[Category: Delft, F von.]]
+[[Category: Edwards A]]
-[[Category: Edwards, A.]]
+[[Category: Eswaran J]]
-[[Category: Eswaran, J.]]
+[[Category: Knapp S]]
-[[Category: Knapp, S.]]
+[[Category: Niesen F]]
-[[Category: Niesen, F.]]
+[[Category: Papagrigoriou E]]
-[[Category: Papagrigoriou, E.]]
+[[Category: Savitsky P]]
-[[Category: SGC, Structural Genomics Consortium.]]
+[[Category: Sundstrom M]]
-[[Category: Savitsky, P.]]
+[[Category: Turnbull A]]
-[[Category: Sundstrom, M.]]
+[[Category: Ugochukwu E]]
-[[Category: Turnbull, A.]]
+[[Category: Weigelt J]]
-[[Category: Ugochukwu, E.]]
+[[Category: Von Delft F]]
-[[Category: Weigelt, J.]]
-[[Category: Glepp1]]
-[[Category: Hydrolase]]
-[[Category: Ptpro]]
-[[Category: Ptpu2]]
-[[Category: Sgc]]
-[[Category: Structural genomic]]
-[[Category: Structural genomics consortium]]
-[[Category: Tyrosine phosphatase]]

2gjt

From Proteopedia

Current revision

Crystal structure of the human receptor phosphatase PTPRO

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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