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==Crystallographic structure of the mature ectodomain of the human receptor-type protein-tyrosine phosphatase IA-2 at 1.30 Angstroms==
==Crystallographic structure of the mature ectodomain of the human receptor-type protein-tyrosine phosphatase IA-2 at 1.30 Angstroms==
<StructureSection load='2qt7' size='340' side='right' caption='[[2qt7]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
<StructureSection load='2qt7' size='340' side='right'caption='[[2qt7]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2qt7]] 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=2QT7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QT7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2qt7]] 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=2QT7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QT7 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 1.3&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PTPRN, ICA3, ICA512 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qt7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qt7 OCA], [https://pdbe.org/2qt7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qt7 RCSB], [https://www.ebi.ac.uk/pdbsum/2qt7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qt7 ProSAT]</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=2qt7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qt7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2qt7 RCSB], [http://www.ebi.ac.uk/pdbsum/2qt7 PDBsum]</span></td></tr>
</table>
<table>
== Function ==
[https://www.uniprot.org/uniprot/PTPRN_HUMAN PTPRN_HUMAN] Implicated in neuroendocrine secretory processes. May be involved in processes specific for neurosecretory granules, such as their biogenesis, trafficking or regulated exocytosis or may have a general role in neuroendocrine functions. Seems to lack intrinsic enzyme activity. May play a role in the regulation of secretory granules via its interaction with SNTB2.<ref>PMID:8144912</ref> <ref>PMID:8641276</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qt/2qt7_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qt/2qt7_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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=2qt7 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
IA-2 (insulinoma-associated protein 2) is a protein-tyrosine phosphatase receptor located in secretory granules of neuroendocrine cells. Initially, it attracted attention due to its involvement in the autoimmune response associated to diabetes. Later it was found that upon exocytosis, the cytoplasmic domain of IA-2 is cleaved and relocated to the nucleus, where it enhances the transcription of the insulin gene. A concerted functioning of the whole receptor is to be expected. However, very little is known about the structure and function of the transmembrane and extracellular domains of IA-2. To address this issue, we solved the x-ray structure of the mature ectodomain of IA-2 (meIA-2) to 1.30A resolution. The fold of meIA-2 is related to the SEA (sea urchin sperm protein, enterokinase, agrin)) domains of mucins, suggesting its participation in adhesive contacts to the extracellular matrix and providing clues on how this kind of molecule may associate and form homo- and heterodimers. Moreover, we discovered that meIA-2 is self-proteolyzed in vitro by reactive oxygen species, suggesting the possibility of a new shedding mechanism that might be significant in normal function or pathological processes. Knowledge of meIA-2 structure should facilitate the search of its possible ligands and molecular interactions.
Structure of the mature ectodomain of the human receptor-type protein-tyrosine phosphatase IA-2.,Primo ME, Klinke S, Sica MP, Goldbaum FA, Jakoncic J, Poskus E, Ermacora MR J Biol Chem. 2008 Feb 22;283(8):4674-81. Epub 2007 Nov 29. PMID:18048354<ref>PMID:18048354</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Tyrosine phosphatase|Tyrosine phosphatase]]
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein-tyrosine-phosphatase]]
[[Category: Large Structures]]
[[Category: Ermacora, M R.]]
[[Category: Ermacora MR]]
[[Category: Goldbaum, F A.]]
[[Category: Goldbaum FA]]
[[Category: Jakoncic, J.]]
[[Category: Jakoncic J]]
[[Category: Klinke, S.]]
[[Category: Klinke S]]
[[Category: Poskus, E.]]
[[Category: Poskus E]]
[[Category: Primo, M E.]]
[[Category: Primo ME]]
[[Category: Sica, M P.]]
[[Category: Sica MP]]
[[Category: Autoimmunity]]
[[Category: Diabetes]]
[[Category: Glycoprotein]]
[[Category: Hydrolase]]
[[Category: Ia-2]]
[[Category: Ica-512]]
[[Category: Protein-tyrosine phosphatase]]
[[Category: Proteolysis]]
[[Category: Receptor]]
[[Category: Transmembrane protein]]

Latest revision as of 12:17, 21 February 2024

Crystallographic structure of the mature ectodomain of the human receptor-type protein-tyrosine phosphatase IA-2 at 1.30 AngstromsCrystallographic structure of the mature ectodomain of the human receptor-type protein-tyrosine phosphatase IA-2 at 1.30 Angstroms

Structural highlights

2qt7 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 1.3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PTPRN_HUMAN Implicated in neuroendocrine secretory processes. May be involved in processes specific for neurosecretory granules, such as their biogenesis, trafficking or regulated exocytosis or may have a general role in neuroendocrine functions. Seems to lack intrinsic enzyme activity. May play a role in the regulation of secretory granules via its interaction with SNTB2.[1] [2]

Evolutionary Conservation

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

See Also

References

  1. ↑ Rabin DU, Pleasic SM, Shapiro JA, Yoo-Warren H, Oles J, Hicks JM, Goldstein DE, Rae PM. Islet cell antigen 512 is a diabetes-specific islet autoantigen related to protein tyrosine phosphatases. J Immunol. 1994 Mar 15;152(6):3183-8. PMID:8144912
  2. ↑ Solimena M, Dirkx R Jr, Hermel JM, Pleasic-Williams S, Shapiro JA, Caron L, Rabin DU. ICA 512, an autoantigen of type I diabetes, is an intrinsic membrane protein of neurosecretory granules. EMBO J. 1996 May 1;15(9):2102-14. PMID:8641276

2qt7, resolution 1.30Å

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