View source for 6l03


==structure of PTP-MEG2 and MUNC18-1-pY145 peptide complex==
<StructureSection load='6l03' size='340' side='right'caption='[[6l03]], [[Resolution|resolution]] 2.08&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6l03]] 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=6L03 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L03 FirstGlance]. <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]] 2.084&#8491;</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6l03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l03 OCA], [https://pdbe.org/6l03 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l03 RCSB], [https://www.ebi.ac.uk/pdbsum/6l03 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l03 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PTN9_HUMAN PTN9_HUMAN] Protein-tyrosine phosphatase that could participate in the transfer of hydrophobic ligands or in functions of the Golgi apparatus.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Tyrosine phosphorylation of secretion machinery proteins is a crucial regulatory mechanism for exocytosis. However, the participation of protein tyrosine phosphatases (PTPs) in different exocytosis stages has not been defined. Here we demonstrate that PTP-MEG2 controls multiple steps of catecholamine secretion. Biochemical and crystallographic analyses reveal key residues that govern the interaction between PTP-MEG2 and its substrate, a peptide containing the phosphorylated NSF-pY(83) site, specify PTP-MEG2 substrate selectivity, and modulate the fusion of catecholamine-containing vesicles. Unexpectedly, delineation of PTP-MEG2 mutants along with the NSF binding interface reveals that PTP-MEG2 controls the fusion pore opening through NSF independent mechanisms. Utilizing bioinformatics search and biochemical and electrochemical screening approaches, we uncover that PTP-MEG2 regulates the opening and extension of the fusion pore by dephosphorylating the DYNAMIN2-pY(125) and MUNC18-1-pY(145) sites. Further structural and biochemical analyses confirmed the interaction of PTP-MEG2 with MUNC18-1-pY(145) or DYNAMIN2-pY(125) through a distinct structural basis compared with that of the NSF-pY(83) site. Our studies thus provide mechanistic insights in complex exocytosis processes.

PTP-MEG2 regulates quantal size and fusion pore opening through two distinct structural bases and substrates.,Xu YF, Chen X, Yang Z, Xiao P, Liu CH, Li KS, Yang XZ, Wang YJ, Zhu ZL, Xu ZG, Zhang S, Wang C, Song YC, Zhao WD, Wang CH, Ji ZL, Zhang ZY, Cui M, Sun JP, Yu X EMBO Rep. 2021 May 5;22(5):e52141. doi: 10.15252/embr.202052141. Epub 2021 Mar , 25. PMID:33764618<ref>PMID:33764618</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6l03" style="background-color:#fffaf0;"></div>

==See Also==
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Chen X]]
[[Category: Sun JP]]
[[Category: Xu YF]]
[[Category: Yu X]]