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- PDB-5yxu: an affinity enhanced T cell receptor in complex with HLA-A0201 re... -

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Basic information

Entry
Database: PDB / ID: 5yxu
Titlean affinity enhanced T cell receptor in complex with HLA-A0201 restricted HCV NS3 peptide KLVALGINAV
Components
  • (T cell receptor ...) x 2
  • Beta-2-microglobulin
  • HLA class I histocompatibility antigen, A-2 alpha chain
  • LYS-LEU-VAL-ALA-LEU-GLY-ILE-ASN-ALA-VAL
KeywordsIMMUNE SYSTEM / affinity enhanced TCR-pHLA complex
Function / homology
Function and homology information


symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT activity / positive regulation of hexokinase activity / translocation of peptides or proteins into host cell cytoplasm / symbiont-mediated perturbation of host cellular process / Toll-like receptor 2 binding / viral capsid assembly / adhesion receptor-mediated virion attachment to host cell / hepacivirin / TBC/RABGAPs / positive regulation of memory T cell activation ...symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT activity / positive regulation of hexokinase activity / translocation of peptides or proteins into host cell cytoplasm / symbiont-mediated perturbation of host cellular process / Toll-like receptor 2 binding / viral capsid assembly / adhesion receptor-mediated virion attachment to host cell / hepacivirin / TBC/RABGAPs / positive regulation of memory T cell activation / T cell mediated cytotoxicity directed against tumor cell target / positive regulation of CD8-positive, alpha-beta T cell activation / CD8-positive, alpha-beta T cell activation / positive regulation of CD8-positive, alpha-beta T cell proliferation / host cell mitochondrial membrane / host cell lipid droplet / symbiont-mediated transformation of host cell / symbiont-mediated suppression of host TRAF-mediated signal transduction / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent / TAP complex binding / antigen processing and presentation of exogenous peptide antigen via MHC class I / Golgi medial cisterna / positive regulation of cytokinesis / symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint / CD8 receptor binding / protection from natural killer cell mediated cytotoxicity / beta-2-microglobulin binding / endoplasmic reticulum exit site / TAP binding / negative regulation of protein secretion / detection of bacterium / antigen processing and presentation of endogenous peptide antigen via MHC class Ib / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent / T cell receptor binding / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity / endoplasmic reticulum-Golgi intermediate compartment membrane / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity / early endosome lumen / Nef mediated downregulation of MHC class I complex cell surface expression / DAP12 interactions / Endosomal/Vacuolar pathway / T cell mediated cytotoxicity / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / lumenal side of endoplasmic reticulum membrane / regulation of iron ion transport / cellular response to iron(III) ion / negative regulation of iron ion transport / negative regulation of forebrain neuron differentiation / antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent / peptide antigen assembly with MHC class I protein complex / ER to Golgi transport vesicle membrane / regulation of erythrocyte differentiation / response to molecule of bacterial origin / HFE-transferrin receptor complex / transferrin transport / MHC class I peptide loading complex / cellular response to iron ion / negative regulation of receptor-mediated endocytosis / positive regulation of T cell cytokine production / antigen processing and presentation of endogenous peptide antigen via MHC class I / MHC class I protein complex / peptide antigen assembly with MHC class II protein complex / negative regulation of neurogenesis / SH3 domain binding / cellular response to nicotine / MHC class II protein complex / positive regulation of receptor-mediated endocytosis / multicellular organismal-level iron ion homeostasis / positive regulation of T cell mediated cytotoxicity / specific granule lumen / antigen processing and presentation of exogenous peptide antigen via MHC class II / positive regulation of immune response / peptide antigen binding / phagocytic vesicle membrane / positive regulation of type II interferon production / recycling endosome membrane / kinase binding / positive regulation of T cell activation / negative regulation of epithelial cell proliferation / Interferon gamma signaling / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / Interferon alpha/beta signaling / Modulation by Mtb of host immune system / sensory perception of smell / positive regulation of cellular senescence / tertiary granule lumen / MHC class II protein complex binding / DAP12 signaling / T cell differentiation in thymus / late endosome membrane / T cell receptor signaling pathway / negative regulation of neuron projection development / nucleoside-triphosphate phosphatase / E3 ubiquitin ligases ubiquitinate target proteins / antibacterial humoral response / protein refolding / ER-Phagosome pathway / viral nucleocapsid / channel activity / early endosome membrane
Similarity search - Function
Hepatitus C virus, Non-structural 5a protein, C-terminal / Hepatitis C virus NS5A, 1B domain superfamily / Hepatitis C virus non-structural protein NS2, C-terminal domain / Hepatitis C virus non-structural protein NS2, N-terminal domain / Hepatitis C virus non-structural protein NS2 / HCV NS5a protein C-terminal region / Hepatitis C virus, Non-structural protein NS4b / Hepatitis C virus, Core protein, N-terminal / Hepatitis C virus core protein, chain A superfamily / : ...Hepatitus C virus, Non-structural 5a protein, C-terminal / Hepatitis C virus NS5A, 1B domain superfamily / Hepatitis C virus non-structural protein NS2, C-terminal domain / Hepatitis C virus non-structural protein NS2, N-terminal domain / Hepatitis C virus non-structural protein NS2 / HCV NS5a protein C-terminal region / Hepatitis C virus, Non-structural protein NS4b / Hepatitis C virus, Core protein, N-terminal / Hepatitis C virus core protein, chain A superfamily / : / Hepatitis C virus non-structural protein NS4b / Hepatitis C virus capsid protein / Hepatitis C virus, Non-structural protein NS2 / Hepatitis C virus, Non-structural 5a protein / Hepatitis C virus, Non-structural 5a protein, domain 1a / Hepatitis C virus non-structural 5a, 1B domain / NS5A domain 1a superfamily / : / Hepatitis C virus non-structural 5a protein membrane anchor / Hepatitis C virus non-structural 5a zinc finger domain / Hepatitis C virus non-structural 5a domain 1b / NS3 RNA helicase, C-terminal helical domain / Hepacivirus nonstructural protein 2 (NS2) protease domain profile. / Hepatitis C virus, Non-structural protein NS4a / Hepatitis C virus non-structural protein NS4a / Hepatitis C virus, Core protein, C-terminal / Hepatitis C virus core protein / Hepatitis C virus, Non-structural protein E2/NS1 / Hepatitis C virus non-structural protein E2/NS1 / Hepatitis C virus, Envelope glycoprotein E1 / Hepatitis C virus envelope glycoprotein E1 / RNA dependent RNA polymerase, hepatitis C virus / Viral RNA dependent RNA polymerase / Hepatitis C virus, NS3 protease, Peptidase S29 / Hepatitis C virus NS3 protease / Hepacivirus/Pegivirus NS3 protease domain profile. / MHC class I, alpha chain, C-terminal / MHC_I C-terminus / MHC class I-like antigen recognition-like / Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1 / DEAD box, Flavivirus / Flavivirus DEAD domain / MHC class I alpha chain, alpha1 alpha2 domains / Class I Histocompatibility antigen, domains alpha 1 and 2 / Beta-2-Microglobulin / : / MHC class I-like antigen recognition-like / MHC class I-like antigen recognition-like superfamily / MHC classes I/II-like antigen recognition protein / : / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin C-Type / Immunoglobulin C1-set / Immunoglobulin C1-set domain / helicase superfamily c-terminal domain / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / Reverse transcriptase/Diguanylate cyclase domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / RNA-directed RNA polymerase, catalytic domain / RdRp of positive ssRNA viruses catalytic domain profile. / Immunoglobulin-like fold / Immunoglobulins / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / DNA/RNA polymerase superfamily / Immunoglobulin-like / Sandwich / P-loop containing nucleoside triphosphate hydrolase / 2-Layer Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
HLA class I histocompatibility antigen, A alpha chain / HLA class I histocompatibility antigen, A alpha chain / Genome polyprotein / Beta-2-microglobulin
Similarity search - Component
Biological speciesHomo sapiens (human)
Hepatitis C virus
MethodX-RAY DIFFRACTION / Resolution: 2.7 Å
AuthorsYi, L.
Funding support China, 3items
OrganizationGrant numberCountry
Science and Technology Program of Guangzhou201504010016 China
the National Key R&D program 2016YFC13034042016YFC1303404 China
cience and Technology Program of Guangzhou201704020220 China
CitationJournal: To Be Published
Title: an affinity enhanced T cell receptor in complex with HLA-A0201 restricted HCV NS3 peptide KLVALGINAV
Authors: Yi, L.
History
DepositionDec 7, 2017Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Dec 12, 2018Provider: repository / Type: Initial release
Revision 1.1Feb 27, 2019Group: Data collection / Derived calculations / Category: pdbx_struct_assembly_gen / pdbx_struct_oper_list
Revision 1.2Oct 9, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
F: T cell receptor alpha chain
G: T cell receptor beta chain
A: T cell receptor alpha chain
B: T cell receptor beta chain
C: HLA class I histocompatibility antigen, A-2 alpha chain
D: Beta-2-microglobulin
E: HLA class I histocompatibility antigen, A-2 alpha chain
H: Beta-2-microglobulin
I: LYS-LEU-VAL-ALA-LEU-GLY-ILE-ASN-ALA-VAL
J: LYS-LEU-VAL-ALA-LEU-GLY-ILE-ASN-ALA-VAL


Theoretical massNumber of molelcules
Total (without water)187,59610
Polymers187,59610
Non-polymers00
Water3,279182
1
E: HLA class I histocompatibility antigen, A-2 alpha chain
H: Beta-2-microglobulin
J: LYS-LEU-VAL-ALA-LEU-GLY-ILE-ASN-ALA-VAL

F: T cell receptor alpha chain
G: T cell receptor beta chain


Theoretical massNumber of molelcules
Total (without water)93,7985
Polymers93,7985
Non-polymers00
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_546-x,y-1/2,-z+11
2
A: T cell receptor alpha chain
B: T cell receptor beta chain
C: HLA class I histocompatibility antigen, A-2 alpha chain
D: Beta-2-microglobulin
I: LYS-LEU-VAL-ALA-LEU-GLY-ILE-ASN-ALA-VAL


Theoretical massNumber of molelcules
Total (without water)93,7985
Polymers93,7985
Non-polymers00
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)60.106, 223.107, 71.855
Angle α, β, γ (deg.)90.000, 98.300, 90.000
Int Tables number4
Space group name H-MP1211

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Components

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T cell receptor ... , 2 types, 4 molecules FAGB

#1: Protein T cell receptor alpha chain


Mass: 21630.986 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli)
#2: Protein T cell receptor beta chain


Mass: 27424.521 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli)

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Protein , 2 types, 4 molecules CEDH

#3: Protein HLA class I histocompatibility antigen, A-2 alpha chain / MHC class I antigen A*2


Mass: 31925.281 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HLA-A, HLAA / Production host: Escherichia coli (E. coli) / References: UniProt: P01892, UniProt: P04439*PLUS
#4: Protein Beta-2-microglobulin


Mass: 11819.173 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P61769*PLUS

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Protein/peptide / Non-polymers , 2 types, 184 molecules IJ

#5: Protein/peptide LYS-LEU-VAL-ALA-LEU-GLY-ILE-ASN-ALA-VAL


Mass: 998.240 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Hepatitis C virus / Production host: Escherichia coli (E. coli) / References: UniProt: P27958*PLUS
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 182 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY

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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: 2.54 Å3/Da / Density % sol: 51.6 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / Details: 15% PEG 3350, 0.2M potassium nitrate

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SEALED TUBE / Type: OXFORD DIFFRACTION ENHANCE ULTRA / Wavelength: 1.54 Å
DetectorType: OXFORD RUBY CCD / Detector: CCD / Date: Jun 3, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.54 Å / Relative weight: 1
ReflectionResolution: 2.7→50 Å / Num. obs: 48316 / % possible obs: 99.5 % / Redundancy: 3.02 % / Net I/σ(I): 6.6
Reflection shellResolution: 2.7→2.85 Å

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Processing

Software
NameVersionClassification
SCALAdata scaling
REFMAC5.8.0049refinement
PDB_EXTRACT3.24data extraction
MOSFLMdata reduction
PHASERphasing
RefinementResolution: 2.7→17.7 Å / Cor.coef. Fo:Fc: 0.876 / Cor.coef. Fo:Fc free: 0.807 / SU B: 18.62 / SU ML: 0.376 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.418
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.2887 2578 5.1 %RANDOM
Rwork0.2352 ---
obs0.238 48315 99.41 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso max: 102.25 Å2 / Biso mean: 29.975 Å2 / Biso min: 2 Å2
Baniso -1Baniso -2Baniso -3
1-1.02 Å2-0 Å2-1.09 Å2
2---1.14 Å2-0 Å2
3---0.42 Å2
Refinement stepCycle: final / Resolution: 2.7→17.7 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13095 0 0 182 13277
Biso mean---18.15 -
Num. residues----1632
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.01913506
X-RAY DIFFRACTIONr_bond_other_d0.0040.0212171
X-RAY DIFFRACTIONr_angle_refined_deg1.4491.92818344
X-RAY DIFFRACTIONr_angle_other_deg1.066328013
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.74851630
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.11423.875689
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.816152190
X-RAY DIFFRACTIONr_dihedral_angle_4_deg21.4651593
X-RAY DIFFRACTIONr_chiral_restr0.0840.21933
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.02115483
X-RAY DIFFRACTIONr_gen_planes_other0.0040.023310
LS refinement shellResolution: 2.7→2.768 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.418 187 -
Rwork0.351 3504 -
all-3691 -
obs--100 %

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