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Open data
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Basic information
Entry | Database: PDB / ID: 1iie | ||||||
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Title | HLA-DR ANTIGENS ASSOCIATED INVARIANT CHAIN | ||||||
![]() | PROTEIN (HLA-DR ANTIGENS ASSOCIATED INVARIANT CHAIN) | ||||||
![]() | MAJOR HISTOCOMPATIBILITY COMPLEX / ANTIGEN PROCESSING / OLIGOMERIZATION / CHAPERONIN | ||||||
Function / homology | ![]() negative regulation of peptide secretion / macrophage migration inhibitory factor signaling pathway / NOS2-CD74 complex / MHC class II protein binding, via antigen binding groove / antigen processing and presentation of endogenous antigen / positive regulation of dendritic cell antigen processing and presentation / negative regulation of T cell differentiation / macrophage migration inhibitory factor binding / positive regulation of macrophage migration inhibitory factor signaling pathway / protein trimerization ...negative regulation of peptide secretion / macrophage migration inhibitory factor signaling pathway / NOS2-CD74 complex / MHC class II protein binding, via antigen binding groove / antigen processing and presentation of endogenous antigen / positive regulation of dendritic cell antigen processing and presentation / negative regulation of T cell differentiation / macrophage migration inhibitory factor binding / positive regulation of macrophage migration inhibitory factor signaling pathway / protein trimerization / macrophage migration inhibitory factor receptor complex / positive regulation of cytokine-mediated signaling pathway / T cell activation involved in immune response / positive regulation of type 2 immune response / T cell selection / negative thymic T cell selection / positive regulation of prostaglandin biosynthetic process / negative regulation of viral entry into host cell / MHC class II protein binding / negative regulation of mature B cell apoptotic process / positive thymic T cell selection / positive regulation of monocyte differentiation / CD4 receptor binding / positive regulation of kinase activity / positive regulation of chemokine (C-X-C motif) ligand 2 production / positive regulation of neutrophil chemotaxis / vacuole / positive regulation of macrophage cytokine production / prostaglandin biosynthetic process / positive regulation of T cell differentiation / cytokine receptor activity / regulation of macrophage activation / transport vesicle membrane / negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / nitric-oxide synthase binding / cytokine binding / response to type II interferon / antigen processing and presentation / negative regulation of DNA damage response, signal transduction by p53 class mediator / chaperone cofactor-dependent protein refolding / immunoglobulin mediated immune response / positive regulation of chemokine production / positive regulation of B cell proliferation / protein folding chaperone / MHC class II antigen presentation / multivesicular body / negative regulation of cell migration / lysosomal lumen / trans-Golgi network membrane / positive regulation of interleukin-8 production / lumenal side of endoplasmic reticulum membrane / Cell surface interactions at the vascular wall / intracellular protein transport / clathrin-coated endocytic vesicle membrane / ER to Golgi transport vesicle membrane / MHC class II protein complex / antigen processing and presentation of exogenous peptide antigen via MHC class II / endocytic vesicle membrane / positive regulation of interleukin-6 production / positive regulation of peptidyl-tyrosine phosphorylation / positive regulation of fibroblast proliferation / late endosome / MHC class II protein complex binding / amyloid-beta binding / protein-containing complex assembly / positive regulation of canonical NF-kappaB signal transduction / positive regulation of MAPK cascade / positive regulation of viral entry into host cell / positive regulation of ERK1 and ERK2 cascade / lysosome / protein stabilization / positive regulation of protein phosphorylation / lysosomal membrane / external side of plasma membrane / Golgi membrane / positive regulation of gene expression / negative regulation of apoptotic process / positive regulation of DNA-templated transcription / cell surface / protein-containing complex / extracellular exosome / identical protein binding / membrane / nucleus / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Jasanoff, A. / Wagner, G. / Wiley, D.C. | ||||||
![]() | ![]() Title: Structure of a trimeric domain of the MHC class II-associated chaperonin and targeting protein Ii. Authors: Jasanoff, A. / Wagner, G. / Wiley, D.C. #1: ![]() Title: An Asymmetric Deuterium Labeling Strategy to Identify Interprotomer and Intraprotomer Noes in Oligomeric Proteins Authors: Jasanoff, A. #2: ![]() Title: Invariant Chain Made in Escherichia coli Has an Exposed N-Terminal Segment that Blocks Antigen Binding to HLA-DR1 and a Trimeric C-Terminal Segment that Binds Empty HLA-DR1 Authors: Park, S.-J. / Sadegh-Nasseri, S. / Wiley, D.C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.4 MB | Display | ![]() |
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PDB format | ![]() | 1.2 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 364 KB | Display | ![]() |
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Full document | ![]() | 718.7 KB | Display | |
Data in XML | ![]() | 121.3 KB | Display | |
Data in CIF | ![]() | 184.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Assembly
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NMR ensembles |
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Components
#1: Protein | Mass: 8984.300 Da / Num. of mol.: 3 Fragment: ECTOPLASMIC TRIMERIZATION DOMAIN (RESIDUES 118-192) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Description: TRYPSIN-GENERATED FRAGMENT OF RECOMBINANT DOMAIN Cellular location: TYPE II TRANSMEMBRANE PROTEIN / Gene: CD74 OR DHLAG / Plasmid: PQE9 / Cellular location (production host): CYTOPLASM / Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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NMR details | Text: THE STRUCTURE WAS DETERMINED USING DOUBLE- AND TRIPLE-RESONANCE EXPERIMENTS ON SAMPLES OF II 118-192 LABELED WITH COMBINATIONS OF 2H, 13C, AND 15N |
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Sample preparation
Sample conditions | pH: 6.7 / Pressure: 1 atm / Temperature: 298 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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Processing
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: THE TRIMER STRUCTURE WAS CALCULATED USING A SIMULATED ANNEALING PROTOCOL BASED ON THE DIMER REFINEMENT METHODS OF NILGES, PROTEINS 17 : 297-309 (1993) | ||||||||||||
NMR ensemble | Conformer selection criteria: LEAST RESTRAINT VIOLATION, GOOD GEOMETRY Conformers calculated total number: 80 / Conformers submitted total number: 20 |