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4neu
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4neu is ON HOLD Authors: Nolte, R.T., Ward, P., kahler, K. M., Campobasso, N. Description: X-ray structure of Receptor Interacting Protein 1 (RIP1)...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==X-ray structure of Receptor Interacting Protein 1 (RIP1)kinase domain with a 1-aminoisoquinoline inhibitor== | |
| - | + | <StructureSection load='4neu' size='340' side='right'caption='[[4neu]], [[Resolution|resolution]] 2.57Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4neu]] is a 2 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=4NEU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NEU FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.57Å</td></tr> | |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=Q1A:1-[4-(1-AMINOISOQUINOLIN-5-YL)PHENYL]-3-(5-TERT-BUTYL-1,2-OXAZOL-3-YL)UREA'>Q1A</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=4neu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4neu OCA], [https://pdbe.org/4neu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4neu RCSB], [https://www.ebi.ac.uk/pdbsum/4neu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4neu ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/RIPK1_HUMAN RIPK1_HUMAN] Serine-threonine kinase which transduces inflammatory and cell-death signals (programmed necrosis) following death receptors ligation, activation of pathogen recognition receptors (PRRs), and DNA damage. Upon activation of TNFR1 by the TNF-alpha family cytokines, TRADD and TRAF2 are recruited to the receptor. Ubiquitination by TRAF2 via 'Lys-63'-link chains acts as a critical enhancer of communication with downstream signal transducers in the mitogen-activated protein kinase pathway and the NF-kappa-B pathway, which in turn mediate downstream events including the activation of genes encoding inflammatory molecules. Polyubiquitinated protein binds to IKBKG/NEMO, the regulatory subunit of the IKK complex, a critical event for NF-kappa-B activation. Interaction with other cellular RHIM-containing adapters initiates gene activation and cell death. RIPK1 and RIPK3 association, in particular, forms a necrosis-inducing complex.<ref>PMID:11101870</ref> <ref>PMID:19524513</ref> <ref>PMID:19524512</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Campobasso N]] | ||
| + | [[Category: Nolte RT]] | ||
| + | [[Category: Ward P]] | ||
| + | [[Category: Kahler KM]] | ||
Current revision
X-ray structure of Receptor Interacting Protein 1 (RIP1)kinase domain with a 1-aminoisoquinoline inhibitor
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