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- PDB-9hr9: SSNMR structure of amyloid fibrils formed by human RIPK1 -

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Basic information

Entry
Database: PDB / ID: 9hr9
TitleSSNMR structure of amyloid fibrils formed by human RIPK1
ComponentsReceptor-interacting serine/threonine-protein kinase 1
KeywordsPROTEIN FIBRIL / Amyloid / kinase
Function / homology
Function and homology information


ripoptosome assembly / positive regulation of miRNA processing / positive regulation of interleukin-6-mediated signaling pathway / death domain binding / ripoptosome assembly involved in necroptotic process / T cell apoptotic process / programmed necrotic cell death / Defective RIPK1-mediated regulated necrosis / Microbial modulation of RIPK1-mediated regulated necrosis / TRIF-mediated programmed cell death ...ripoptosome assembly / positive regulation of miRNA processing / positive regulation of interleukin-6-mediated signaling pathway / death domain binding / ripoptosome assembly involved in necroptotic process / T cell apoptotic process / programmed necrotic cell death / Defective RIPK1-mediated regulated necrosis / Microbial modulation of RIPK1-mediated regulated necrosis / TRIF-mediated programmed cell death / ripoptosome / Regulation by c-FLIP / CASP8 activity is inhibited / Dimerization of procaspase-8 / TLR3-mediated TICAM1-dependent programmed cell death / activation of protein kinase activity / positive regulation of macrophage differentiation / TNF signaling / Caspase activation via Death Receptors in the presence of ligand / SARS-CoV-1-mediated effects on programmed cell death / necroptotic process / negative regulation of necroptotic process / JUN kinase kinase kinase activity / necroptotic signaling pathway / NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10 / RIP-mediated NFkB activation via ZBP1 / death-inducing signaling complex / positive regulation of necroptotic process / Dengue virus modulates apoptosis / positive regulation of tumor necrosis factor-mediated signaling pathway / death receptor binding / positive regulation of programmed necrotic cell death / positive regulation of extrinsic apoptotic signaling pathway / TNFR1-induced proapoptotic signaling / RIPK1-mediated regulated necrosis / positive regulation of programmed cell death / extrinsic apoptotic signaling pathway via death domain receptors / TRP channels / protein serine/threonine phosphatase activity / response to tumor necrosis factor / negative regulation of extrinsic apoptotic signaling pathway in absence of ligand / positive regulation of execution phase of apoptosis / extrinsic apoptotic signaling pathway / canonical NF-kappaB signal transduction / signaling adaptor activity / negative regulation of extrinsic apoptotic signaling pathway / tumor necrosis factor-mediated signaling pathway / negative regulation of canonical NF-kappaB signal transduction / positive regulation of interleukin-8 production / TICAM1, RIP1-mediated IKK complex recruitment / protein serine/threonine kinase binding / IKK complex recruitment mediated by RIP1 / cellular response to tumor necrosis factor / intrinsic apoptotic signaling pathway in response to DNA damage / TNFR1-induced NF-kappa-B signaling pathway / Regulation of TNFR1 signaling / positive regulation of non-canonical NF-kappaB signal transduction / cellular response to growth factor stimulus / positive regulation of JNK cascade / cellular response to hydrogen peroxide / Regulation of necroptotic cell death / positive regulation of reactive oxygen species metabolic process / positive regulation of inflammatory response / positive regulation of neuron apoptotic process / positive regulation of tumor necrosis factor production / Ovarian tumor domain proteases / response to oxidative stress / amyloid fibril formation / Potential therapeutics for SARS / positive regulation of canonical NF-kappaB signal transduction / protein kinase activity / non-specific serine/threonine protein kinase / signaling receptor complex / endosome membrane / intracellular signal transduction / Ub-specific processing proteases / positive regulation of apoptotic process / inflammatory response / protein serine kinase activity / ubiquitin protein ligase binding / protein serine/threonine kinase activity / apoptotic process / positive regulation of gene expression / negative regulation of apoptotic process / protein-containing complex binding / positive regulation of transcription by RNA polymerase II / protein homodimerization activity / protein-containing complex / mitochondrion / ATP binding / identical protein binding / plasma membrane / cytosol / cytoplasm
Similarity search - Function
RIP1, Death domain / Death domain profile. / DEATH domain, found in proteins involved in cell death (apoptosis). / Death domain / Death domain / : / Death-like domain superfamily / Protein tyrosine and serine/threonine kinase / Serine-threonine/tyrosine-protein kinase, catalytic domain / Serine/threonine-protein kinase, active site ...RIP1, Death domain / Death domain profile. / DEATH domain, found in proteins involved in cell death (apoptosis). / Death domain / Death domain / : / Death-like domain superfamily / Protein tyrosine and serine/threonine kinase / Serine-threonine/tyrosine-protein kinase, catalytic domain / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Serine/Threonine protein kinases, catalytic domain / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily
Similarity search - Domain/homology
Receptor-interacting serine/threonine-protein kinase 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLID-STATE NMR / molecular dynamics
AuthorsPolonio, P. / Escobedo-Gonzales, F.C. / Titaux-Delgado, G.A. / Mompean, M.
Funding supportEuropean Union, 1items
OrganizationGrant numberCountry
European Research Council (ERC)101042403European Union
CitationJournal: Biomol.Nmr Assign. / Year: 2025
Title: Resonance assignments of the human receptor interacting protein kinase 1 (RIPK1) in its fibrillar conformation.
Authors: Polonio, P. / Mompean, M.
History
DepositionDec 17, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 17, 2025Provider: repository / Type: Initial release
Revision 1.1Oct 1, 2025Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Oct 22, 2025Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Receptor-interacting serine/threonine-protein kinase 1


Theoretical massNumber of molelcules
Total (without water)2,5141
Polymers2,5141
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: NMR Distance Restraints, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 100target function
RepresentativeModel #1lowest energy

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Components

#1: Protein/peptide Receptor-interacting serine/threonine-protein kinase 1 / Cell death protein RIP / Receptor-interacting protein 1 / RIP-1


Mass: 2513.842 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RIPK1, RIP, RIP1 / Plasmid: pET11a / Production host: Escherichia coli BL21(DE3) (bacteria)
References: UniProt: Q13546, non-specific serine/threonine protein kinase
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: SOLID-STATE NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDSample stateSpectrometer-IDType
111isotropic1NCACX
121isotropic1NCOCX
131isotropic1CANCOCX
141isotropic1CORD 20 ms
151isotropic1CORD 50 ms
161isotropic1CORD 100 ms
171isotropic1CORD 500 ms

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Sample preparation

DetailsType: fibrous protein
Contents: 25 % w/w [U-100% 13C; U-100% 15N] protein, 75 % w/w None protein, 100% H2O
Details: 1:4 labelled:unlabelled hRIPK1 (RHIM) / Label: 13C15_diluted / Solvent system: 100% H2O
SampleConc.: 25 % w/w / Component: protein / Isotopic labeling: [U-100% 13C; U-100% 15N]
Sample conditionsDetails: Fibrils in water at pH 7.4 (dialyzed from 20 mM Tris)
Ionic strength: 0 mM / Label: conditions_1 / pH: 7.4 / Pressure: 1 atm / Temperature: 310 K / Temperature err: 1

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NMR measurement

NMR spectrometerType: Bruker AVANCE NEO / Manufacturer: Bruker / Model: AVANCE NEO / Field strength: 600 MHz / Details: HCN CPMAS CryoProbe

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Processing

NMR software
NameDeveloperClassification
CYANAGuntert, Mumenthaler and Wuthrichstructure calculation
GROMACShttps://doi.org/10.5281/zenodo.11148638refinement
CcpNmr AnalysisCCPNchemical shift assignment
RefinementMethod: molecular dynamics / Software ordinal: 2
Details: 100 structures calculated with cyana and 10 lowest-energy conformers refined using GROMACS
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 10

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