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6kc4

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(New page: '''Unreleased structure''' The entry 6kc4 is ON HOLD Authors: Description: Category: Unreleased Structures)
Current revision (10:29, 22 November 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 6kc4 is ON HOLD
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==Crystal structure of human Fer SH2 domain bound to a phosphopeptide (DEpYENVD)==
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<StructureSection load='6kc4' size='340' side='right'caption='[[6kc4]], [[Resolution|resolution]] 1.37&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6kc4]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KC4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KC4 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.37&#8491;</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6kc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kc4 OCA], [https://pdbe.org/6kc4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kc4 RCSB], [https://www.ebi.ac.uk/pdbsum/6kc4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kc4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FER_HUMAN FER_HUMAN] Tyrosine-protein kinase that acts downstream of cell surface receptors for growth factors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, lamellipodia formation, cell adhesion, cell migration and chemotaxis. Acts downstream of EGFR, KIT, PDGFRA and PDGFRB. Acts downstream of EGFR to promote activation of NF-kappa-B and cell proliferation. May play a role in the regulation of the mitotic cell cycle. Plays a role in the insulin receptor signaling pathway and in activation of phosphatidylinositol 3-kinase. Acts downstream of the activated FCER1 receptor and plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Plays a role in the regulation of mast cell degranulation. Plays a role in leukocyte recruitment and diapedesis in response to bacterial lipopolysaccharide (LPS). Plays a role in synapse organization, trafficking of synaptic vesicles, the generation of excitatory postsynaptic currents and neuron-neuron synaptic transmission. Plays a role in neuronal cell death after brain damage. Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1 and PTPN11. May phosphorylate JUP and PTPN1. Can phosphorylate STAT3, but the biological relevance of this depends on cell type and stimulus.<ref>PMID:22223638</ref> <ref>PMID:7623846</ref> <ref>PMID:9722593</ref> <ref>PMID:12972546</ref> <ref>PMID:14517306</ref> <ref>PMID:19339212</ref> <ref>PMID:19147545</ref> <ref>PMID:19738202</ref> <ref>PMID:20111072</ref> <ref>PMID:21518868</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Fes and Fes-related (Fer) protein tyrosine kinases (PTKs) comprise a subfamily of nonreceptor tyrosine kinases characterized by a unique multidomain structure composed of an N-terminal Fer/CIP4 homology-Bin/Amphiphysin/Rvs (F-BAR) domain, a central Src homology 2 (SH2) domain, and a C-terminal PTK domain. Fer is ubiquitously expressed, and upregulation of Fer has been implicated in various human cancers. The PTK activity of Fes has been shown to be positively regulated by the binding of phosphotyrosine-containing ligands to the SH2 domain. Here, the X-ray crystal structure of human Fer SH2 domain bound to a phosphopeptide that has D-E-pY-E-N-V-D sequence is reported at 1.37 a resolution. The asymmetric unit (ASU) contains six Fer-phosphopeptide complexes, and the structure reveals three distinct binding modes for the same phosphopeptide. At four out of the six binding sites in the ASU, the phosphopeptide binds to Fer SH2 domain in a type I beta-turn conformation, and this could be the optimal binding mode of this phosphopeptide. At the other two binding sites in the ASU, it appears that spatial proximity of neighboring SH2 domains in the crystal induces alternative modes of binding of this phosphopeptide.
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Authors:
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High-resolution structural analysis shows how different crystallographic environments can induce alternative modes of binding of a phosphotyrosine peptide to the SH2 domain of Fer tyrosine kinase.,Matsuura Y Protein Sci. 2019 Nov;28(11):2011-2019. doi: 10.1002/pro.3713. Epub 2019 Aug 31. PMID:31441171<ref>PMID:31441171</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6kc4" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Tyrosine kinase 3D structures|Tyrosine kinase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Synthetic construct]]
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[[Category: Matsuura Y]]

Current revision

Crystal structure of human Fer SH2 domain bound to a phosphopeptide (DEpYENVD)

PDB ID 6kc4

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