[English] 日本語
Yorodumi
- PDB-8ddd: Intramembrane recognition between transmembrane domains of IL-9R ... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 8ddd
TitleIntramembrane recognition between transmembrane domains of IL-9R and common gamma chain
Components
  • Cytokine receptor common subunit gamma
  • Interleukin-9 receptor
KeywordsMEMBRANE PROTEIN / common gamma-chain cytokine receptor / transmembrane domain / receptor sharing
Function / homology
Function and homology information


interleukin-9 receptor activity / interleukin-9 binding / Interleukin-2 signaling / Interleukin-21 signaling / Interleukin-9 signaling / Interleukin-4 and Interleukin-13 signaling / mature B cell differentiation / Interleukin-15 signaling / interleukin-15 receptor activity / interleukin-2 binding ...interleukin-9 receptor activity / interleukin-9 binding / Interleukin-2 signaling / Interleukin-21 signaling / Interleukin-9 signaling / Interleukin-4 and Interleukin-13 signaling / mature B cell differentiation / Interleukin-15 signaling / interleukin-15 receptor activity / interleukin-2 binding / CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation / Interleukin-7 signaling / Interleukin receptor SHC signaling / RAF/MAP kinase cascade / positive regulation of T cell differentiation in thymus / lymphocyte differentiation / interleukin-9-mediated signaling pathway / positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation / interleukin-2-mediated signaling pathway / interleukin-15-mediated signaling pathway / cytokine receptor activity / positive regulation of B cell differentiation / B cell proliferation / cytokine binding / immunoglobulin mediated immune response / coreceptor activity / regulation of peptidyl-tyrosine phosphorylation / positive regulation of phagocytosis / B cell differentiation / cytokine-mediated signaling pathway / gene expression / T cell differentiation in thymus / regulation of gene expression / positive regulation of cell growth / receptor complex / external side of plasma membrane / positive regulation of gene expression / cell surface / endoplasmic reticulum / extracellular region / nucleoplasm / plasma membrane
Similarity search - Function
: / : / Cytokine receptor-like factor 2-like, D2 domain / Cytokine receptor-like factor 2, domain 1 / Short hematopoietin receptor family 1 signature. / Short hematopoietin receptor, family 1, conserved site / Fibronectin type 3 domain / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Immunoglobulin-like fold
Similarity search - Domain/homology
Cytokine receptor common subunit gamma / Interleukin-9 receptor
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodSOLUTION NMR / simulated annealing
AuthorsLenoir Capello, R. / Cai, T. / Chou, J.J.
Funding support United States, 3items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM140887 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)AI150709 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM132079 United States
CitationJournal: Science / Year: 2023
Title: Structural basis of gamma chain family receptor sharing at the membrane level.
Authors: Cai, T. / Lenoir Capello, R. / Pi, X. / Wu, H. / Chou, J.J.
History
DepositionJun 17, 2022Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 5, 2023Provider: repository / Type: Initial release
Revision 1.1Aug 30, 2023Group: Data collection / Database references
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID
Revision 1.2May 15, 2024Group: Database references / Category: database_2 / Item: _database_2.pdbx_DOI

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Cytokine receptor common subunit gamma
B: Interleukin-9 receptor


Theoretical massNumber of molelcules
Total (without water)7,4052
Polymers7,4052
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: NMR Distance Restraints, Inter-molecular NOEs
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area960 Å2
ΔGint-14 kcal/mol
Surface area6380 Å2
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)15 / 100structures with the lowest energy
RepresentativeModel #1lowest energy

-
Components

#1: Protein/peptide Cytokine receptor common subunit gamma / Interleukin-2 receptor subunit gamma / IL-2 receptor subunit gamma / IL-2R subunit gamma / IL-2RG / ...Interleukin-2 receptor subunit gamma / IL-2 receptor subunit gamma / IL-2R subunit gamma / IL-2RG / gammaC / p64


Mass: 3864.547 Da / Num. of mol.: 1 / Fragment: Transmembrane domain, residues 253-286 / Mutation: M271V, C282F
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Il2rg / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P34902
#2: Protein/peptide Interleukin-9 receptor / IL-9 receptor / IL-9R


Mass: 3540.373 Da / Num. of mol.: 1 / Fragment: Transmembrane domain, residues 268-298
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Il9r / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / Variant (production host): C43 / References: UniProt: Q01114

-
Experimental details

-
Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDSample stateSpectrometer-IDType
111isotropic12D 1H-15N TROSY-HSQC
122isotropic12D 1H-15N TROSY-HSQC
133isotropic42D 1H-15N TROSY-HSQC
144isotropic42D 1H-15N TROSY-HSQC
153isotropic42D 1H-13C HSQC
164isotropic42D 1H-13C HSQC
171isotropic13D TROSY HNCA
182isotropic13D TROSY HNCA
191isotropic13D TROSY HN(CO)CA
1102isotropic13D TROSY HN(CO)CA
1111isotropic13D TROSY HNCO
1122isotropic13D TROSY HNCO
1131isotropic13D TROSY HN(CA)CO
1142isotropic13D TROSY HN(CA)CO
1153isotropic43D 1H-15N NOESY-TROSY
1164isotropic43D 1H-15N NOESY-TROSY
1175isotropic43D 1H-15N NOESY-TROSY
1183isotropic43D 1H-13C NOESY
1194isotropic43D 1H-13C NOESY
1205isotropic43D 1H-13C NOESY
1213isotropic22D Methyl-Amide Intermolecular NOESY

-
Sample preparation

Details
TypeSolution-IDContentsDetailsLabelSolvent system
bicelle10.4 mM 15N, 13C, 85%2H Transmembrane domain of the common gamma-chain receptor, 40 mM DMPC, 100 mM DH6PC, 90% H2O/10% D2O(15N,13C,85%2H)-labeled gamma-chain TMD in DMPC-DHPC Bicelles (q=0.4) for triple resonance experiments.gC(15N,13C,85%2H)90% H2O/10% D2O
bicelle20.4 mM 15N, 13C, 85%2H Transmembrane domain of the Interleukin-9 receptor alpha subunit, 40 mM DMPC, 100 mM DH6PC, 90% H2O/10% D2O(15N,13C,85%2H)-labeled IL-9 receptor TMD in DMPC-DHPC Bicelles (q=0.4) for triple resonance experiments.9R(15N,13C,85%2H)90% H2O/10% D2O
bicelle30.4 mM 13C Transmembrane domain of the Interleukin-9 receptor alpha subunit, 0.4 mM 15N, 2H Transmembrane domain of the common gamma-chain receptor, 80 mM deuterated DMPC, 200 mM deuterated DH6PC, 90% H2O/10% D2O(15N,2H)-labeled gamma chain TMD mixed with (13C)-labeled IL-9 receptor TMD at 1:1 molar ratio in DMPC-DHPC Bicelles (q=0.4) for detecting inter-molecular NOEs.gC(15N,2H)-9R(13C)90% H2O/10% D2O
bicelle40.4 mM 13C Transmembrane domain of the common gamma-chain receptor, 0.4 mM 15N, 2H Transmembrane domain of the Interleukin-9 receptor alpha subunit, 80 mM deuterated DMPC, 200 mM deuterated DH6PC, 90% H2O/10% D2O(15N,2H)-labeled IL-9 receptor TMD mixed with (13C)-labeled gamma-chain TMD at 1:1 molar ratio in DMPC-DHPC Bicelles (q=0.4) for detecting inter-molecular NOEs.9R(15N,2H)-gC(13C)90% H2O/10% D2O
bicelle50.4 mM 13C Transmembrane domain of the Interleukin-9 receptor alpha subunit, 0.4 mM 15N, 2H Transmembrane domain of the common gamma-chain receptor, 80 mM deuterated DMPC, 200 mM deuterated DH6PC, 90% H2O/10% D2O(15N,13C)-labeled IL-9 receptor TMD mixed with (15N-13C)-labeled gamma-chain TMD at 1:1 molar ratio in DMPC-DHPC Bicelles (q=0.4) for detecting inter-molecular NOEs.9R(15N,13C)-gC(15N-13C)90% H2O/10% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
0.4 mMTransmembrane domain of the common gamma-chain receptor15N, 13C, 85%2H1
40 mMDMPCnatural abundance1
100 mMDH6PCnatural abundance1
0.4 mMTransmembrane domain of the Interleukin-9 receptor alpha subunit15N, 13C, 85%2H2
40 mMDMPCnatural abundance2
100 mMDH6PCnatural abundance2
0.4 mMTransmembrane domain of the Interleukin-9 receptor alpha subunit13C3
0.4 mMTransmembrane domain of the common gamma-chain receptor15N, 2H3
80 mMDMPCdeuterated3
200 mMDH6PCdeuterated3
0.4 mMTransmembrane domain of the common gamma-chain receptor13C4
0.4 mMTransmembrane domain of the Interleukin-9 receptor alpha subunit15N, 2H4
80 mMDMPCdeuterated4
200 mMDH6PCdeuterated4
0.4 mMTransmembrane domain of the Interleukin-9 receptor alpha subunit13C5
0.4 mMTransmembrane domain of the common gamma-chain receptor15N, 2H5
80 mMDMPCdeuterated5
200 mMDH6PCdeuterated5
Sample conditionsDetails: The condition used for all NMR data collection / Ionic strength: 0.15 M / Label: NMR measurements / pH: 6.7 / Pressure: 1 atm / Pressure err: 0.01 / Temperature: 303 K / Temperature err: 0.1

-
NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AVANCE IIIBrukerAVANCE III6001
Bruker AVANCE NEOBrukerAVANCE NEO7002
Bruker AVANCE IIIBrukerAVANCE III8004

-
Processing

NMR software
NameDeveloperClassification
NMRPipeDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Baxprocessing
XEASYBartels et al.chemical shift assignment
TALOS+Shen, Delaglio, Cornilescu, Baxchemical shift calculation
X-PLOR NIHSchwieters, Kuszewski, Tjandra and Clorerefinement
RefinementMethod: simulated annealing / Software ordinal: 5
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 15

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more