1ivo
From Proteopedia
(Difference between revisions)
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<StructureSection load='1ivo' size='340' side='right'caption='[[1ivo]], [[Resolution|resolution]] 3.30Å' scene=''> | <StructureSection load='1ivo' size='340' side='right'caption='[[1ivo]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1ivo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1ivo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The June 2010 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Epidermal Growth Factor Receptor'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2010_6 10.2210/rcsb_pdb/mom_2010_6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IVO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IVO FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3Å</td></tr> |
- | <tr id=' | + | <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> |
- | + | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ivo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ivo OCA], [https://pdbe.org/1ivo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ivo RCSB], [https://www.ebi.ac.uk/pdbsum/1ivo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ivo ProSAT], [https://www.topsan.org/Proteins/RSGI/1ivo TOPSAN]</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=1ivo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ivo OCA], [https://pdbe.org/1ivo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ivo RCSB], [https://www.ebi.ac.uk/pdbsum/1ivo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ivo ProSAT], [https://www.topsan.org/Proteins/RSGI/1ivo TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
- | + | [https://www.uniprot.org/uniprot/EGFR_HUMAN EGFR_HUMAN] Defects in EGFR are associated with lung cancer (LNCR) [MIM:[https://omim.org/entry/211980 211980]. LNCR is a common malignancy affecting tissues of the lung. The most common form of lung cancer is non-small cell lung cancer (NSCLC) that can be divided into 3 major histologic subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung cancer. NSCLC is often diagnosed at an advanced stage and has a poor prognosis. | |
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/EGFR_HUMAN EGFR_HUMAN] Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. Known ligands include EGF, TGFA/TGF-alpha, amphiregulin, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF. Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules. May also activate the NF-kappa-B signaling cascade. Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling. Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin.<ref>PMID:7657591</ref> <ref>PMID:11602604</ref> <ref>PMID:12873986</ref> <ref>PMID:10805725</ref> <ref>PMID:11116146</ref> <ref>PMID:11483589</ref> <ref>PMID:17115032</ref> <ref>PMID:21258366</ref> <ref>PMID:12297050</ref> <ref>PMID:12620237</ref> <ref>PMID:15374980</ref> <ref>PMID:19560417</ref> <ref>PMID:20837704</ref> Isoform 2 may act as an antagonist of EGF action.<ref>PMID:7657591</ref> <ref>PMID:11602604</ref> <ref>PMID:12873986</ref> <ref>PMID:10805725</ref> <ref>PMID:11116146</ref> <ref>PMID:11483589</ref> <ref>PMID:17115032</ref> <ref>PMID:21258366</ref> <ref>PMID:12297050</ref> <ref>PMID:12620237</ref> <ref>PMID:15374980</ref> <ref>PMID:19560417</ref> <ref>PMID:20837704</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Epidermal Growth Factor Receptor]] | [[Category: Epidermal Growth Factor Receptor]] | ||
- | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
- | + | [[Category: Fukai S]] | |
- | [[Category: Fukai | + | [[Category: Ishitani R]] |
- | [[Category: Ishitani | + | [[Category: Kim JH]] |
- | [[Category: Kim | + | [[Category: Nureki O]] |
- | [[Category: Nureki | + | [[Category: Ogiso H]] |
- | [[Category: Ogiso | + | [[Category: Saito K]] |
- | + | [[Category: Shirouzu M]] | |
- | [[Category: Saito | + | [[Category: Yamanaka M]] |
- | [[Category: Shirouzu | + | [[Category: Yokoyama S]] |
- | [[Category: Yamanaka | + | |
- | [[Category: Yokoyama | + | |
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Revision as of 23:37, 27 December 2023
Crystal Structure of the Complex of Human Epidermal Growth Factor and Receptor Extracellular Domains.
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