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5ul6

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==The molecular mechanisms by which NS1 of the 1918 Spanish influenza A virus hijack host protein-protein interactions==
==The molecular mechanisms by which NS1 of the 1918 Spanish influenza A virus hijack host protein-protein interactions==
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<StructureSection load='5ul6' size='340' side='right' caption='[[5ul6]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
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<StructureSection load='5ul6' size='340' side='right'caption='[[5ul6]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5ul6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UL6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UL6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5ul6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Influenza_A_virus Influenza A virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UL6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UL6 FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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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]] 1.45&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ul6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ul6 OCA], [http://pdbe.org/5ul6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ul6 RCSB], [http://www.ebi.ac.uk/pdbsum/5ul6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ul6 ProSAT]</span></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=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=5ul6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ul6 OCA], [https://pdbe.org/5ul6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ul6 RCSB], [https://www.ebi.ac.uk/pdbsum/5ul6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ul6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CRK_HUMAN CRK_HUMAN]] The Crk-I and Crk-II forms differ in their biological activities. Crk-II has less transforming activity than Crk-I. Crk-II mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4. May regulate the EFNA5-EPHA3 signaling.<ref>PMID:1630456</ref> <ref>PMID:11870224</ref> <ref>PMID:17515907</ref>
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[https://www.uniprot.org/uniprot/CRK_HUMAN CRK_HUMAN] The Crk-I and Crk-II forms differ in their biological activities. Crk-II has less transforming activity than Crk-I. Crk-II mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4. May regulate the EFNA5-EPHA3 signaling.<ref>PMID:1630456</ref> <ref>PMID:11870224</ref> <ref>PMID:17515907</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5ul6" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5ul6" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Adapter molecule crk 3D structures|Adapter molecule crk 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cho, J H]]
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[[Category: Homo sapiens]]
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[[Category: Li, P]]
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[[Category: Influenza A virus]]
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[[Category: Shen, Q]]
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[[Category: Large Structures]]
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[[Category: Zeng, D]]
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[[Category: Cho JH]]
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[[Category: Zhao, B]]
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[[Category: Li P]]
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[[Category: Crkii]]
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[[Category: Shen Q]]
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[[Category: Influenza a virus]]
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[[Category: Zeng D]]
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[[Category: Nonstructural protein 1]]
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[[Category: Zhao B]]
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[[Category: Sh3]]
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[[Category: Viral protein]]
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Current revision

The molecular mechanisms by which NS1 of the 1918 Spanish influenza A virus hijack host protein-protein interactions

PDB ID 5ul6

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