2i75: Difference between revisions
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<StructureSection load='2i75' size='340' side='right'caption='[[2i75]], [[Resolution|resolution]] 2.45Å' scene=''> | <StructureSection load='2i75' size='340' side='right'caption='[[2i75]], [[Resolution|resolution]] 2.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2i75]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2i75]] is a 1 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=2I75 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I75 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id=' | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2i75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i75 OCA], [https://pdbe.org/2i75 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i75 RCSB], [https://www.ebi.ac.uk/pdbsum/2i75 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i75 ProSAT]</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=2i75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i75 OCA], [https://pdbe.org/2i75 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i75 RCSB], [https://www.ebi.ac.uk/pdbsum/2i75 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i75 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/PTN4_HUMAN PTN4_HUMAN] May act at junctions between the membrane and the cytoskeleton. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Arrowsmith C]] | |||
[[Category: Arrowsmith | [[Category: Barr A]] | ||
[[Category: Barr | [[Category: Burgess N]] | ||
[[Category: Burgess | [[Category: Das S]] | ||
[[Category: Das | [[Category: Edwards A]] | ||
[[Category: Knapp S]] | |||
[[Category: Edwards | [[Category: Savitsky P]] | ||
[[Category: Knapp | [[Category: Sundstrom M]] | ||
[[Category: Turnbull A]] | |||
[[Category: Savitsky | [[Category: Ugochukwu E]] | ||
[[Category: Sundstrom | [[Category: Weigelt J]] | ||
[[Category: Turnbull | [[Category: Von Delft F]] | ||
[[Category: Ugochukwu | |||
[[Category: Weigelt | |||
[[Category: | |||
Latest revision as of 13:07, 30 August 2023
Crystal Structure of Human Protein Tyrosine Phosphatase N4 (PTPN4)Crystal Structure of Human Protein Tyrosine Phosphatase N4 (PTPN4)
Structural highlights
FunctionPTN4_HUMAN May act at junctions between the membrane and the cytoskeleton. 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 PubMedProtein 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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