4aw4: Difference between revisions

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<StructureSection load='4aw4' size='340' side='right'caption='[[4aw4]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
<StructureSection load='4aw4' size='340' side='right'caption='[[4aw4]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4aw4]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Lismo Lismo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AW4 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4aw4]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes_EGD-e Listeria monocytogenes EGD-e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AW4 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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]] 1.93&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1d0b|1d0b]], [[1h6t|1h6t]], [[1m9s|1m9s]], [[1otm|1otm]], [[1otn|1otn]], [[1oto|1oto]], [[2uzx|2uzx]], [[2uzy|2uzy]], [[2wqu|2wqu]], [[2wqv|2wqv]], [[2wqw|2wqw]], [[2wqx|2wqx]], [[2y5p|2y5p]], [[2y5q|2y5q]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=4aw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aw4 OCA], [https://pdbe.org/4aw4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aw4 RCSB], [https://www.ebi.ac.uk/pdbsum/4aw4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aw4 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=4aw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aw4 OCA], [https://pdbe.org/4aw4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aw4 RCSB], [https://www.ebi.ac.uk/pdbsum/4aw4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aw4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/INLB_LISMO INLB_LISMO]] Mediates the entry of Listeria monocytogenes into cells.  
[https://www.uniprot.org/uniprot/INLB_LISMG INLB_LISMG] Mediates the entry of L.monocytogenes into normally non-phagocytic mammalian host cells (Probable) (PubMed:9282740, PubMed:11081636). Its host receptor is hepatocyte growth factor receptor (HGF receptor, a tyrosine kinase, MET) which is tyrosine-phosphorylated in response to InlB in human, green monkey, mouse and dog cell lines (PubMed:11081636, PubMed:15049825). Downstream adapter proteins GAB1 and CBL are phosphorylated in response to InlB, which also causes cell colony scattering (PubMed:11081636). InlB binding to mammalian cells is saturable and inhibited by EDTA; InlB-coated beads can be taken up by host cells (PubMed:10747014). Complement component 1 Q subcomponent-binding protein (gC1q-R, C1QBP) might act as an InlB receptor, leading to activation of PI3-kinase in green monkey cells (PubMed:10747014). Stimulation of Tyr-phosphorylation by InlB is antagonized by C1QBP, showing that potentiation of MET signaling via the GW domains is not mediated by C1QBP; the exact role of C1QBP remains to be determined (PubMed:15049825). Stimulation of Tyr-phosphorylation of MET by InlB is potentiated by the InlB GW domains and glycosaminoglycans such as heparin; exogenously added InlB, or hepatocyte growth factor (HGF) will also substitute for bacterial InlB, suggesting InlB promotes bacterial invasion by mimicking the hormone HGF (PubMed:15049825). May stimulate phosphatidylinositol 4,5-bisphosphate 3-kinase (PI3-kinase) in green monkey cells, has less effect in humans as PI3-kinase is constitutively and highly expressed in Caco cells (Probable). Binds heparin; C1QBP and heparin seem to bind to the GW domains (PubMed:12411480).<ref>PMID:10747014</ref> <ref>PMID:11081636</ref> <ref>PMID:12411480</ref> <ref>PMID:15049825</ref> <ref>PMID:9282740</ref> <ref>PMID:11081636</ref> <ref>PMID:1905979</ref> <ref>PMID:8864117</ref>
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lismo]]
[[Category: Listeria monocytogenes EGD-e]]
[[Category: Heinz, D W]]
[[Category: Heinz DW]]
[[Category: Niemann, H H]]
[[Category: Niemann HH]]
[[Category: C-met ligand]]
[[Category: Cell invasion]]
[[Category: Hgf receptor ligand]]
[[Category: Lrr]]
[[Category: Protein binding]]
[[Category: Protein engineering]]
[[Category: Protein protein interaction]]
[[Category: Receptor binding]]
[[Category: Virulence factor]]

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