4exp

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[[Image:4exp.png|left|200px]]
 
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==Structure of mouse Interleukin-34 in complex with mouse FMS==
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The line below this paragraph, containing "STRUCTURE_4exp", creates the "Structure Box" on the page.
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<StructureSection load='4exp' size='340' side='right'caption='[[4exp]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[4exp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EXP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EXP 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]] 2.8&#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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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{{STRUCTURE_4exp| PDB=4exp | SCENE= }}
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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=4exp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4exp OCA], [https://pdbe.org/4exp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4exp RCSB], [https://www.ebi.ac.uk/pdbsum/4exp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4exp ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CSF1R_MOUSE CSF1R_MOUSE] Tyrosine-protein kinase that acts as cell-surface receptor for CSF1 and IL34 and plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, especially mononuclear phagocytes, such as macrophages and monocytes. Promotes the release of proinflammatory chemokines in response to IL34 and CSF1, and thereby plays an important role in innate immunity and in inflammatory processes. Plays an important role in the regulation of osteoclast proliferation and differentiation, the regulation of bone resorption, and is required for normal bone and tooth development. Required for normal male and female fertility, and for normal development of milk ducts and acinar structures in the mammary gland during pregnancy. Promotes reorganization of the actin cytoskeleton, regulates formation of membrane ruffles, cell adhesion and cell migration, and promotes cancer cell invasion. Activates several signaling pathways in response to ligand binding. Phosphorylates PIK3R1, PLCG2, GRB2, SLA2 and CBL. Activation of PLCG2 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, that then lead to the activation of protein kinase C family members, especially PRKCD. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to activation of the AKT1 signaling pathway. Activated CSF1R also mediates activation of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1, and of the SRC family kinases SRC, FYN and YES1. Activated CSF1R transmits signals both via proteins that directly interact with phosphorylated tyrosine residues in its intracellular domain, or via adapter proteins, such as GRB2. Promotes activation of STAT family members STAT3, STAT5A and/or STAT5B. Promotes tyrosine phosphorylation of SHC1 and INPP5D/SHIP-1. Receptor signaling is down-regulated by protein phosphatases, such as INPP5D/SHIP-1, that dephosphorylate the receptor and its downstream effectors, and by rapid internalization of the activated receptor.<ref>PMID:1652061</ref> <ref>PMID:8262059</ref> <ref>PMID:8007983</ref> <ref>PMID:9312046</ref> <ref>PMID:10958675</ref> <ref>PMID:11756160</ref> <ref>PMID:16950670</ref> <ref>PMID:17353186</ref> <ref>PMID:17420255</ref> <ref>PMID:17420256</ref> <ref>PMID:17972959</ref> <ref>PMID:18814279</ref> <ref>PMID:20181277</ref> <ref>PMID:20504948</ref> <ref>PMID:21727904</ref> <ref>PMID:21610095</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Interleukin-34 (IL-34) and colony stimulating factor-1 (CSF-1) both signal through the CSF-1R receptor tyrosine kinase, but they have no sequence homology, and their functions and signaling activities are not identical. We report the crystal structures of mouse IL-34 alone and in complex with the N-terminal three immunoglobulin-like domains (D1-D3) of mouse CSF-1R. IL-34 is structurally related to other helical hematopoietic cytokines, but contains two additional helices integrally associated with the four shared helices. The non-covalently linked IL-34 homodimer recruits two copies of CSF-1R on the sides of the helical bundles, with an overall shape similar to the CSF-1:CSF-1R complex, but the flexible linker between CSF-1R D2 and D3 allows these domains to clamp IL-34 and CSF-1 at different angles. Functional dissection of the IL-34:CSF-1R interface indicates that the hydrophobic interactions, rather than the salt bridge network, dominate the biological activity of IL-34. To degenerately recognize two ligands with completely different surfaces, CSF-1R apparently takes advantage of different subsets of a chemically inert surface that can be tuned to fit different ligand shapes. Differentiated signaling between IL-34 and CSF-1 is likely achieved by the relative thermodynamic independence of IL-34 vs. negative cooperativity of CSF-1 at the receptor-recognition sites, in combination with the difference in hydrophobicity which dictates a more stable IL-34:CSF-1R complex compared to the CSF-1:CSF-1R complex.
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===Structure of mouse Interleukin-34 in complex with mouse FMS===
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The mechanism of shared but distinct CSF-1R signaling by the non-homologous cytokines IL-34 and CSF-1.,Liu H, Leo C, Chen X, Wong BR, Williams LT, Lin H, He X Biochim Biophys Acta. 2012 May 8. PMID:22579672<ref>PMID:22579672</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4exp" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_22579672}}, adds the Publication Abstract to the page
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*[[Colony-stimulating factor receptor 3D structures|Colony-stimulating factor receptor 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 22579672 is the PubMed ID number.
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*[[Interleukin 3D structures|Interleukin 3D structures]]
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== References ==
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{{ABSTRACT_PUBMED_22579672}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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[[4exp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EXP OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:022579672</ref><references group="xtra"/>
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Receptor protein-tyrosine kinase]]
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[[Category: Chen X]]
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[[Category: Chen, X.]]
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[[Category: He X]]
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[[Category: He, X.]]
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[[Category: Leo C]]
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[[Category: Leo, C.]]
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[[Category: Lin H]]
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[[Category: Lin, H.]]
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[[Category: Liu H]]
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[[Category: Liu, H.]]
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[[Category: Williams LT]]
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[[Category: Williams, L T.]]
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[[Category: Wong BR]]
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[[Category: Wong, B R.]]
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[[Category: Beta-sandwich]]
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[[Category: Cytokine-transferase complex]]
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[[Category: Extended 4-helix bundle]]
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[[Category: Immunoglobunin]]
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Current revision

Structure of mouse Interleukin-34 in complex with mouse FMS

PDB ID 4exp

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