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- PDB-1d01: STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A H... -

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Basic information

Entry
Database: PDB / ID: 1d01
TitleSTRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A HUMAN CD30 PEPTIDE
Components
  • CD30 PEPTIDE
  • TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2
KeywordsAPOPTOSIS / B-SANDWICH / PROTEIN-PEPTIDE COMPLEX
Function / homology
Function and homology information


CD40 receptor binding / positive regulation of TRAIL production / tumor necrosis factor receptor superfamily complex / sphingolipid binding / IRE1-TRAF2-ASK1 complex / Defective RIPK1-mediated regulated necrosis / TRAF2-GSTP1 complex / negative regulation of glial cell apoptotic process / TNFs bind their physiological receptors / Regulation by c-FLIP ...CD40 receptor binding / positive regulation of TRAIL production / tumor necrosis factor receptor superfamily complex / sphingolipid binding / IRE1-TRAF2-ASK1 complex / Defective RIPK1-mediated regulated necrosis / TRAF2-GSTP1 complex / negative regulation of glial cell apoptotic process / TNFs bind their physiological receptors / Regulation by c-FLIP / CASP8 activity is inhibited / Dimerization of procaspase-8 / tumor necrosis factor binding / TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway / interleukin-17-mediated signaling pathway / programmed necrotic cell death / TNF signaling / Caspase activation via Death Receptors in the presence of ligand / CD40 receptor complex / signal transduction involved in regulation of gene expression / activation of NF-kappaB-inducing kinase activity / vesicle membrane / mitogen-activated protein kinase kinase kinase binding / positive regulation of tumor necrosis factor-mediated signaling pathway / mRNA stabilization / thioesterase binding / tumor necrosis factor receptor binding / positive regulation of extrinsic apoptotic signaling pathway / regulation of immunoglobulin production / TNFR1-induced proapoptotic signaling / RIPK1-mediated regulated necrosis / TRAF6 mediated IRF7 activation / non-canonical NF-kappaB signal transduction / TRAF6 mediated NF-kB activation / protein K63-linked ubiquitination / regulation of JNK cascade / intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress / cellular response to nitric oxide / regulation of protein-containing complex assembly / protein autoubiquitination / signaling adaptor activity / ubiquitin ligase complex / positive regulation of JUN kinase activity / tumor necrosis factor-mediated signaling pathway / positive regulation of interleukin-2 production / response to endoplasmic reticulum stress / TNFR1-induced NF-kappa-B signaling pathway / Regulation of NF-kappa B signaling / TNFR2 non-canonical NF-kB pathway / Regulation of TNFR1 signaling / protein catabolic process / RING-type E3 ubiquitin transferase / Regulation of necroptotic cell death / cytoplasmic side of plasma membrane / positive regulation of T cell cytokine production / positive regulation of DNA-binding transcription factor activity / cellular response to mechanical stimulus / ubiquitin-protein transferase activity / transmembrane signaling receptor activity / positive regulation of tumor necrosis factor production / protein-macromolecule adaptor activity / positive regulation of NF-kappaB transcription factor activity / cell cortex / protein-containing complex assembly / regulation of apoptotic process / protein phosphatase binding / positive regulation of canonical NF-kappaB signal transduction / membrane => GO:0016020 / molecular adaptor activity / Ub-specific processing proteases / positive regulation of apoptotic process / membrane raft / negative regulation of cell population proliferation / innate immune response / ubiquitin protein ligase binding / protein-containing complex binding / protein kinase binding / enzyme binding / signal transduction / zinc ion binding / extracellular exosome / nucleoplasm / identical protein binding / plasma membrane / cytoplasm / cytosol
Similarity search - Function
Tumour necrosis factor receptor 8 / Tumour necrosis factor receptor 8, N-terminal / TNF receptor-associated factor 2 / TNF receptor-associated factor 2, MATH domain / : / TRAF2, second zinc finger / TNF receptor-associated factor, BIRC3 binding domain / TNF receptor-associated factor BIRC3 binding domain / TRAF-type zinc finger / TNF receptor-associated factor TRAF, metazoa ...Tumour necrosis factor receptor 8 / Tumour necrosis factor receptor 8, N-terminal / TNF receptor-associated factor 2 / TNF receptor-associated factor 2, MATH domain / : / TRAF2, second zinc finger / TNF receptor-associated factor, BIRC3 binding domain / TNF receptor-associated factor BIRC3 binding domain / TRAF-type zinc finger / TNF receptor-associated factor TRAF, metazoa / Zinc finger, TRAF-type / Zinc finger TRAF-type profile. / : / TRAF/meprin, MATH domain / Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A / Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A / TNFR/NGFR family cysteine-rich region domain profile. / TNFR/NGFR cysteine-rich region / TNFR/NGFR family cysteine-rich region signature. / Tumor necrosis factor receptor / nerve growth factor receptor repeats. / TNFR/NGFR cysteine-rich region / MATH/TRAF domain / MATH/TRAF domain profile. / meprin and TRAF homology / TRAF-like / Zinc finger, C3HC4 RING-type / Zinc finger, C3HC4 type (RING finger) / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / Ring finger / Zinc finger RING-type profile. / Zinc finger, RING-type / Zinc finger, RING/FYVE/PHD-type / Sandwich / Mainly Beta
Similarity search - Domain/homology
Tumor necrosis factor receptor superfamily member 8 / TNF receptor-associated factor 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2 Å
AuthorsYe, H. / Park, Y.C. / Kreishman, M. / Kieff, E. / Wu, H.
Citation
Journal: Mol.Cell / Year: 1999
Title: The structural basis for the recognition of diverse receptor sequences by TRAF2.
Authors: Ye, H. / Park, Y.C. / Kreishman, M. / Kieff, E. / Wu, H.
#1: Journal: Nature / Year: 1999
Title: Structural basis for self-association and receptor recognition of human TRAF2
Authors: Park, Y.C. / Burkitt, V. / Villa, A.R. / Tong, L. / Wu, H.
History
DepositionSep 7, 1999Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 2, 2003Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 4, 2017Group: Refinement description / Category: software
Revision 1.4Jan 31, 2018Group: Experimental preparation / Category: exptl_crystal_grow / Item: _exptl_crystal_grow.temp

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2
B: TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2
C: TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2
D: TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2
E: TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2
F: TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2
G: CD30 PEPTIDE
H: CD30 PEPTIDE
I: CD30 PEPTIDE


Theoretical massNumber of molelcules
Total (without water)116,9559
Polymers116,9559
Non-polymers00
Water14,898827
1
A: TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2
B: TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2
C: TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2


Theoretical massNumber of molelcules
Total (without water)57,0993
Polymers57,0993
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3250 Å2
ΔGint-22 kcal/mol
Surface area22740 Å2
MethodPISA
2
D: TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2
E: TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2
F: TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2
G: CD30 PEPTIDE
H: CD30 PEPTIDE
I: CD30 PEPTIDE


Theoretical massNumber of molelcules
Total (without water)59,8566
Polymers59,8566
Non-polymers00
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6970 Å2
ΔGint-39 kcal/mol
Surface area23100 Å2
MethodPISA
Unit cell
Length a, b, c (Å)91.300, 110.400, 91.300
Angle α, β, γ (deg.)90.00, 120.00, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein
TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2 / TRAF2


Mass: 19032.953 Da / Num. of mol.: 6 / Fragment: TRAF DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: PET24D / Production host: Escherichia coli (E. coli) / References: UniProt: Q12933
#2: Protein/peptide CD30 PEPTIDE


Mass: 919.009 Da / Num. of mol.: 3 / Fragment: TRAF-BINDING SEQUENCE / Source method: obtained synthetically
Details: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE OF THIS PEPTIDE NATURALLY OCCURS IN HUMANS (HOMO SAPIENS)
References: UniProt: P28908
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 827 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3.41 Å3/Da / Density % sol: 63.88 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 6
Details: PEG4K, MES, PH 6.0, VAPOR DIFFUSION, temperature 20K
Crystal grow
*PLUS
pH: 6 / Method: unknown
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
18-15 %PEG400011
20.1 MMES11

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Data collection

DiffractionMean temperature: 110 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X4A / Wavelength: 1.018
DetectorType: ADSC / Detector: CCD / Date: Feb 1, 1999
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.018 Å / Relative weight: 1
ReflectionResolution: 2→20 Å / Num. obs: 94994 / % possible obs: 96.5 % / Rmerge(I) obs: 0.061
Reflection shellHighest resolution: 2 Å / Rmerge(I) obs: 0.199 / % possible all: 93.8
Reflection shell
*PLUS
% possible obs: 93.8 %

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Processing

Software
NameClassification
DENZOdata reduction
SCALEPACKdata scaling
CNSrefinement
RefinementResolution: 2→20 Å / σ(F): 2 / σ(I): 0
RfactorNum. reflection
Rfree0.244 -
Rwork0.22 -
obs0.22 85296
Refinement stepCycle: LAST / Resolution: 2→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7878 0 0 827 8705
Refinement
*PLUS
Rfactor Rwork: 0.22
Solvent computation
*PLUS
Displacement parameters
*PLUS

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