5k5x: Difference between revisions

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<StructureSection load='5k5x' size='340' side='right'caption='[[5k5x]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
<StructureSection load='5k5x' size='340' side='right'caption='[[5k5x]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5k5x]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K5X OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5K5X FirstGlance]. <br>
<table><tr><td colspan='2'>[[5k5x]] 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=5K5X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K5X FirstGlance]. <br>
</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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.168&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] </span></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5k5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k5x OCA], [http://pdbe.org/5k5x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k5x RCSB], [http://www.ebi.ac.uk/pdbsum/5k5x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k5x 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=5k5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k5x OCA], [https://pdbe.org/5k5x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k5x RCSB], [https://www.ebi.ac.uk/pdbsum/5k5x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k5x ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[http://www.uniprot.org/uniprot/PGFRA_HUMAN PGFRA_HUMAN]] Myeloid neoplasm associated with PDGFRA rearrangement;Primary hypereosinophilic syndrome;Precursor B-cell acute lymphoblastic leukemia;Gastrointestinal stromal tumor. A chromosomal aberration involving PDGFRA is found in some cases of hypereosinophilic syndrome. Interstitial chromosomal deletion del(4)(q12q12) causes the fusion of FIP1L1 and PDGFRA (FIP1L1-PDGFRA). Mutations that cause overexpression and/or constitutive activation of PDGFRA may be a cause of hypereosinophilic syndrome.<ref>PMID:12808148</ref>  The gene represented in this entry may be involved in disease pathogenesis. Mutations causing PDGFRA constitutive activation have been found in gastrointestinal stromal tumors lacking KIT mutations (PubMed:12522257).<ref>PMID:12522257</ref>
[https://www.uniprot.org/uniprot/PGFRA_HUMAN PGFRA_HUMAN] Myeloid neoplasm associated with PDGFRA rearrangement;Primary hypereosinophilic syndrome;Precursor B-cell acute lymphoblastic leukemia;Gastrointestinal stromal tumor. A chromosomal aberration involving PDGFRA is found in some cases of hypereosinophilic syndrome. Interstitial chromosomal deletion del(4)(q12q12) causes the fusion of FIP1L1 and PDGFRA (FIP1L1-PDGFRA). Mutations that cause overexpression and/or constitutive activation of PDGFRA may be a cause of hypereosinophilic syndrome.<ref>PMID:12808148</ref>  The gene represented in this entry may be involved in disease pathogenesis. Mutations causing PDGFRA constitutive activation have been found in gastrointestinal stromal tumors lacking KIT mutations (PubMed:12522257).<ref>PMID:12522257</ref>  
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PGFRA_HUMAN PGFRA_HUMAN]] Tyrosine-protein kinase that acts as a cell-surface receptor for PDGFA, PDGFB and PDGFC and plays an essential role in the regulation of embryonic development, cell proliferation, survival and chemotaxis. Depending on the context, promotes or inhibits cell proliferation and cell migration. Plays an important role in the differentiation of bone marrow-derived mesenchymal stem cells. Required for normal skeleton development and cephalic closure during embryonic development. Required for normal development of the mucosa lining the gastrointestinal tract, and for recruitment of mesenchymal cells and normal development of intestinal villi. Plays a role in cell migration and chemotaxis in wound healing. Plays a role in platelet activation, secretion of agonists from platelet granules, and in thrombin-induced platelet aggregation. Binding of its cognate ligands - homodimeric PDGFA, homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFC -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PIK3R1, PLCG1, and PTPN11. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylates PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and thereby mediates activation of the AKT1 signaling pathway. Mediates activation of HRAS and of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3 and STAT5A and/or STAT5B. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor.<ref>PMID:10734113</ref> <ref>PMID:10947961</ref> <ref>PMID:11297552</ref> <ref>PMID:12522257</ref> <ref>PMID:1646396</ref> <ref>PMID:1709159</ref> <ref>PMID:17141222</ref> <ref>PMID:20972453</ref> <ref>PMID:21224473</ref> <ref>PMID:21596750</ref> <ref>PMID:2554309</ref> <ref>PMID:8188664</ref> <ref>PMID:8760137</ref> <ref>PMID:8943348</ref>
[https://www.uniprot.org/uniprot/PGFRA_HUMAN PGFRA_HUMAN] Tyrosine-protein kinase that acts as a cell-surface receptor for PDGFA, PDGFB and PDGFC and plays an essential role in the regulation of embryonic development, cell proliferation, survival and chemotaxis. Depending on the context, promotes or inhibits cell proliferation and cell migration. Plays an important role in the differentiation of bone marrow-derived mesenchymal stem cells. Required for normal skeleton development and cephalic closure during embryonic development. Required for normal development of the mucosa lining the gastrointestinal tract, and for recruitment of mesenchymal cells and normal development of intestinal villi. Plays a role in cell migration and chemotaxis in wound healing. Plays a role in platelet activation, secretion of agonists from platelet granules, and in thrombin-induced platelet aggregation. Binding of its cognate ligands - homodimeric PDGFA, homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFC -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PIK3R1, PLCG1, and PTPN11. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylates PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and thereby mediates activation of the AKT1 signaling pathway. Mediates activation of HRAS and of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3 and STAT5A and/or STAT5B. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor.<ref>PMID:10734113</ref> <ref>PMID:10947961</ref> <ref>PMID:11297552</ref> <ref>PMID:12522257</ref> <ref>PMID:1646396</ref> <ref>PMID:1709159</ref> <ref>PMID:17141222</ref> <ref>PMID:20972453</ref> <ref>PMID:21224473</ref> <ref>PMID:21596750</ref> <ref>PMID:2554309</ref> <ref>PMID:8188664</ref> <ref>PMID:8760137</ref> <ref>PMID:8943348</ref>  
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
*[[Platelet-derived growth factors and receptors|Platelet-derived growth factors and receptors]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Receptor protein-tyrosine kinase]]
[[Category: Liang L]]
[[Category: Liang, L]]
[[Category: Yan XE]]
[[Category: Yan, X E]]
[[Category: Yun CH]]
[[Category: Yun, C H]]
[[Category: Autoinhibition]]
[[Category: Transferase]]
[[Category: Tyrosine kinase]]

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