4s0g: Difference between revisions

Latest revision as of 15:16, 8 November 2023

Crystal structure of PTPN3 (PTPH1) in complex with Eps15 pTyr849 P850V peptide

Structural highlights

4s0g 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 1.723Å
Ligands:	PTR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PTN3_HUMAN May act at junctions between the membrane and the cytoskeleton. Possesses tyrosine phosphatase activity.

Publication Abstract from PubMed

Epidermal growth factor receptor (EGFR) pathway substrate 15 (Eps15) is a newly identified substrate for protein tyrosine phosphatase N3 (PTPN3), which belongs to the FERM-containing PTP subfamily comprising five members including PTPN3, N4, N13, N14, and N21. We solved the crystal structures of the PTPN3-Eps15 phosphopeptide complex and found that His812 of PTPN3 and Pro850 of Eps15 are responsible for the specific interaction between them. We defined the critical role of the additional residue Tyr676 of PTPN3, which is replaced by Ile939 in PTPN14, in recognition of tyrosine phosphorylated Eps15. The WPD loop necessary for catalysis is present in all members but not PTPN21. We identified that Glu instead of Asp in the WPE loop contributes to the catalytic incapability of PTPN21 due to an extended distance beyond protonation targeting a phosphotyrosine substrate. Together with in vivo validations, our results provide novel insights into the substrate specificity and plasticity of FERM-containing PTPs.

Substrate Specificity and Plasticity of FERM-Containing Protein Tyrosine Phosphatases.,Chen KE, Li MY, Chou CC, Ho MR, Chen GC, Meng TC, Wang AH Structure. 2015 Feb 18. pii: S0969-2126(15)00041-6. doi:, 10.1016/j.str.2015.01.017. PMID:25728925^[1]

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

References

↑ Chen KE, Li MY, Chou CC, Ho MR, Chen GC, Meng TC, Wang AH. Substrate Specificity and Plasticity of FERM-Containing Protein Tyrosine Phosphatases. Structure. 2015 Feb 18. pii: S0969-2126(15)00041-6. doi:, 10.1016/j.str.2015.01.017. PMID:25728925 doi:https://dx.doi.org/10.1016/j.str.2015.01.017

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OCA

[1] Chen KE, Li MY, Chou CC, Ho MR, Chen GC, Meng TC, Wang AH. Substrate Specificity and Plasticity of FERM-Containing Protein Tyrosine Phosphatases. Structure. 2015 Feb 18. pii: S0969-2126(15)00041-6. doi:, 10.1016/j.str.2015.01.017. PMID:25728925 doi:https://dx.doi.org/10.1016/j.str.2015.01.017

[1]

@@ Line 3: / Line 3: @@
 <StructureSection load='4s0g' size='340' side='right'caption='[[4s0g]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4s0g]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4S0G FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4s0g]] 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=4S0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4S0G FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.723&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2b49|2b49]], [[4rh5|4rh5]], [[4ri4|4ri4]], [[4ri5|4ri5]], [[4rhg|4rhg]], [[4rh9|4rh9]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [https://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=4s0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s0g OCA], [https://pdbe.org/4s0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4s0g RCSB], [https://www.ebi.ac.uk/pdbsum/4s0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4s0g ProSAT]</span></td></tr>
 </table>
-== Disease ==
-[[https://www.uniprot.org/uniprot/EPS15_HUMAN EPS15_HUMAN]] Note=A chromosomal aberration involving EPS15 is found in acute leukemias. Translocation t(1;11)(p32;q23) with MLL/HRX. The result is a rogue activator protein.
 == Function ==
-[[https://www.uniprot.org/uniprot/PTN3_HUMAN PTN3_HUMAN]] May act at junctions between the membrane and the cytoskeleton. Possesses tyrosine phosphatase activity. [[https://www.uniprot.org/uniprot/EPS15_HUMAN EPS15_HUMAN]] Involved in cell growth regulation. May be involved in the regulation of mitogenic signals and control of cell proliferation. Involved in the internalization of ligand-inducible receptors of the receptor tyrosine kinase (RTK) type, in particular EGFR. Plays a role in the assembly of clathrin-coated pits (CCPs). Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2.<ref>PMID:18362181</ref> <ref>PMID:19458185</ref> <ref>PMID:22648170</ref> <ref>PMID:16903783</ref>
+[https://www.uniprot.org/uniprot/PTN3_HUMAN PTN3_HUMAN] May act at junctions between the membrane and the cytoskeleton. Possesses tyrosine phosphatase activity.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 29: / Line 26: @@
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Protein-tyrosine-phosphatase]]
+[[Category: Chen K-E]]
-[[Category: Chen, K E]]
+[[Category: Meng TC]]
-[[Category: Meng, T C]]
+[[Category: Wang AH-J]]
-[[Category: Wang, A H.J]]
-[[Category: Alpha beta]]
-[[Category: Hydrolase]]
-[[Category: Hydrolase-protein binding complex]]

4s0g: Difference between revisions

Latest revision as of 15:16, 8 November 2023

Crystal structure of PTPN3 (PTPH1) in complex with Eps15 pTyr849 P850V peptide

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

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