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1q7x

From Proteopedia

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Current revision

Solution structure of the alternatively spliced PDZ2 domain (PDZ2b) of PTP-Bas (hPTP1E)

Structural highlights

1q7x is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PTN13_HUMAN Tyrosine phosphatase which regulates negatively FAS-induced apoptosis and NGFR-mediated pro-apoptotic signaling.^[1]

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

Two versions of the PDZ2 domain of the protein tyrosine phosphatase PTP-Bas/human PTP-BL are generated by alternative splicing. The domains differ by the insertion of five amino acid residues and their affinity to the tumour suppressor protein APC. Whereas PDZ2a is able to bind APC in the nanomolar range, PDZ2b shows no apparent interaction with APC. Here the solution structure of the splicing variant of PDZ2 with the insertion has been determined using 2D and 3D heteronuclear NMR experiments. The structural reason for the changed binding specificity is the reorientation of the loop with extra five amino acid residues, which folds back onto beta-strands two and three. In addition the side-chain of Lys32 closes the binding site of the APC binding protein and the two helices, especially alpha-helix 2, change their relative position to the protein core. Consecutively, the binding site is sterically no longer fully accessible. From the NMR-titration studies with a C-terminal APC-peptide the affinity of the peptide with the protein can be estimated as 540(+/-40)microM. The binding site encompasses part of the analogous binding site of PDZ2a as already described previously, yet specific interaction sites are abolished by the insertion of amino acids in PDZ2b. As shown by high-affinity chromatography, GST-PDZ2b and GST-PDZ2a bind to phosphatidylinositol 4,5-bisphosphate (PIP(2)) micelles with a dissociation constant K(D) of 21 microM and 55 microM, respectively. In line with these data PDZ2b binds isolated, dissolved PIP(2) and PIP(3) (phosphatidylinositol 3,4,5-trisphosphate) molecules specifically with a lower K(D) of 230(+/-20)microM as detected by NMR spectroscopy. The binding site could be located by our studies and involves the residues Ile24, Val26, Val70, Asn71, Gly77, Ala78, Glu85, Arg88, Gly91 and Gln92. PIP(2) and PIP(3) binding takes place in the groove of the PDZ domain that is normally part of the APC binding site.

Structure determination and ligand interactions of the PDZ2b domain of PTP-Bas (hPTP1E): splicing-induced modulation of ligand specificity.,Kachel N, Erdmann KS, Kremer W, Wolff P, Gronwald W, Heumann R, Kalbitzer HR J Mol Biol. 2003 Nov 14;334(1):143-55. PMID:14596806^[2]

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

References

↑ Villa F, Deak M, Bloomberg GB, Alessi DR, van Aalten DM. Crystal structure of the PTPL1/FAP-1 human tyrosine phosphatase mutated in colorectal cancer: evidence for a second phosphotyrosine substrate recognition pocket. J Biol Chem. 2005 Mar 4;280(9):8180-7. Epub 2004 Dec 20. PMID:15611135 doi:10.1074/jbc.M412211200
↑ Kachel N, Erdmann KS, Kremer W, Wolff P, Gronwald W, Heumann R, Kalbitzer HR. Structure determination and ligand interactions of the PDZ2b domain of PTP-Bas (hPTP1E): splicing-induced modulation of ligand specificity. J Mol Biol. 2003 Nov 14;334(1):143-55. PMID:14596806

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1q7x"

@@ Line 1: / Line 1: @@
 ==Solution structure of the alternatively spliced PDZ2 domain (PDZ2b) of PTP-Bas (hPTP1E)==
-<StructureSection load='1q7x' size='340' side='right' caption='[[1q7x]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1q7x' size='340' side='right'caption='[[1q7x]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1q7x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q7X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q7X FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1q7x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q7X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q7X FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PTP1E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-<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=1q7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q7x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1q7x RCSB], [http://www.ebi.ac.uk/pdbsum/1q7x PDBsum]</span></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=1q7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q7x OCA], [https://pdbe.org/1q7x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q7x RCSB], [https://www.ebi.ac.uk/pdbsum/1q7x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q7x ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PTN13_HUMAN PTN13_HUMAN]] Tyrosine phosphatase which regulates negatively FAS-induced apoptosis and NGFR-mediated pro-apoptotic signaling.<ref>PMID:15611135</ref>
+[https://www.uniprot.org/uniprot/PTN13_HUMAN PTN13_HUMAN] Tyrosine phosphatase which regulates negatively FAS-induced apoptosis and NGFR-mediated pro-apoptotic signaling.<ref>PMID:15611135</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/q7/1q7x_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q7/1q7x_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=1q7x ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 26: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1q7x" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 31: / Line 33: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Erdmann, K S]]
+[[Category: Large Structures]]
-[[Category: Gronwald, W]]
+[[Category: Erdmann KS]]
-[[Category: Heumann, R]]
+[[Category: Gronwald W]]
-[[Category: Kachel, N]]
+[[Category: Heumann R]]
-[[Category: Kalbitzer, H R]]
+[[Category: Kachel N]]
-[[Category: Kremer, W]]
+[[Category: Kalbitzer HR]]
-[[Category: SPINE, Structural Proteomics in Europe]]
+[[Category: Kremer W]]
-[[Category: Wolff, P]]
+[[Category: Wolff P]]
-[[Category: Hydrolase]]
-[[Category: Phosphatase]]
-[[Category: Spine]]
-[[Category: Structural genomic]]
-[[Category: Structural proteomics in europe]]

1q7x

From Proteopedia

Current revision

Solution structure of the alternatively spliced PDZ2 domain (PDZ2b) of PTP-Bas (hPTP1E)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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