2qep: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2qep]] 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=2QEP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QEP FirstGlance]. <br>
<table><tr><td colspan='2'>[[2qep]] 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=2QEP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QEP 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2i1y|2i1y]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2i1y|2i1y]]</td></tr>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PTPRN2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PTPRN2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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>
<tr id='activity'><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>
<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=2qep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qep OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2qep RCSB], [http://www.ebi.ac.uk/pdbsum/2qep PDBsum]</span></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=2qep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qep OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2qep RCSB], [http://www.ebi.ac.uk/pdbsum/2qep PDBsum]</span></td></tr>
<table>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/PTPR2_HUMAN PTPR2_HUMAN]] Implicated in development of nervous system and pancreatic endocrine cells.<ref>PMID:8878534</ref> <ref>PMID:8798755</ref> 
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein-tyrosine-phosphatase]]
[[Category: Protein-tyrosine-phosphatase]]
[[Category: Alfano, I.]]
[[Category: Alfano, I]]
[[Category: Arrowsmith, C H.]]
[[Category: Arrowsmith, C H]]
[[Category: Barr, A.]]
[[Category: Barr, A]]
[[Category: Berridge, G.]]
[[Category: Berridge, G]]
[[Category: Bunkoczi, G.]]
[[Category: Bunkoczi, G]]
[[Category: Burgess-Brown, N.]]
[[Category: Burgess-Brown, N]]
[[Category: Das, S.]]
[[Category: Das, S]]
[[Category: Delft, F von.]]
[[Category: Delft, F von]]
[[Category: Edwards, A.]]
[[Category: Edwards, A]]
[[Category: Fedorov, O.]]
[[Category: Fedorov, O]]
[[Category: King, O.]]
[[Category: King, O]]
[[Category: Knapp, S.]]
[[Category: Knapp, S]]
[[Category: Niesen, F.]]
[[Category: Niesen, F]]
[[Category: Pike, A C.W.]]
[[Category: Pike, A C.W]]
[[Category: SGC, Structural Genomics Consortium.]]
[[Category: Structural genomic]]
[[Category: Salah, E.]]
[[Category: Salah, E]]
[[Category: Savitsky, P.]]
[[Category: Savitsky, P]]
[[Category: Sundstrom, M.]]
[[Category: Sundstrom, M]]
[[Category: Ugochukwu, E.]]
[[Category: Ugochukwu, E]]
[[Category: Watt, S.]]
[[Category: Watt, S]]
[[Category: Weigelt, J.]]
[[Category: Weigelt, J]]
[[Category: Autoantigen]]
[[Category: Autoantigen]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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[[Category: Ptprp]]
[[Category: Ptprp]]
[[Category: Sgc]]
[[Category: Sgc]]
[[Category: Structural genomic]]
[[Category: Structural genomics consortium]]

Revision as of 00:03, 26 December 2014

Crystal structure of the D1 domain of PTPRN2 (IA2beta)Crystal structure of the D1 domain of PTPRN2 (IA2beta)

Structural highlights

2qep 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.
Ligands:
Gene:PTPRN2 (Homo sapiens)
Activity:Protein-tyrosine-phosphatase, with EC number 3.1.3.48
Resources:FirstGlance, OCA, RCSB, PDBsum

Function

[PTPR2_HUMAN] Implicated in development of nervous system and pancreatic endocrine cells.[1] [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.

See Also

References

  1. ↑ Kawasaki E, Hutton JC, Eisenbarth GS. Molecular cloning and characterization of the human transmembrane protein tyrosine phosphatase homologue, phogrin, an autoantigen of type 1 diabetes. Biochem Biophys Res Commun. 1996 Oct 14;227(2):440-7. PMID:8878534 doi:S0006-291X(96)91526-0
  2. ↑ Cui L, Yu WP, DeAizpurua HJ, Schmidli RS, Pallen CJ. Cloning and characterization of islet cell antigen-related protein-tyrosine phosphatase (PTP), a novel receptor-like PTP and autoantigen in insulin-dependent diabetes. J Biol Chem. 1996 Oct 4;271(40):24817-23. PMID:8798755
  3. ↑ 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

2qep, resolution 2.50Å

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