[English] 日本語
Yorodumi
- PDB-5xr1: Structure of FLN IG21 domain in complex with C-terminal peptide o... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5xr1
TitleStructure of FLN IG21 domain in complex with C-terminal peptide of beta-2
ComponentsC-terminal peptide of Integrin beta-2,Filamin-A IG21 domain
KeywordsSIGNALING PROTEIN / Integrin / cytosolic tail
Function / homology
Function and homology information


integrin alphaX-beta2 complex / regulation of membrane repolarization during atrial cardiac muscle cell action potential / regulation of membrane repolarization during cardiac muscle cell action potential / establishment of Sertoli cell barrier / positive regulation of prostaglandin-E synthase activity / positive regulation of neutrophil degranulation / integrin alphaM-beta2 complex / Myb complex / integrin alphaL-beta2 complex / glycoprotein Ib-IX-V complex ...integrin alphaX-beta2 complex / regulation of membrane repolarization during atrial cardiac muscle cell action potential / regulation of membrane repolarization during cardiac muscle cell action potential / establishment of Sertoli cell barrier / positive regulation of prostaglandin-E synthase activity / positive regulation of neutrophil degranulation / integrin alphaM-beta2 complex / Myb complex / integrin alphaL-beta2 complex / glycoprotein Ib-IX-V complex / adenylate cyclase-inhibiting dopamine receptor signaling pathway / formation of radial glial scaffolds / ICAM-3 receptor activity / positive regulation of integrin-mediated signaling pathway / cytoplasmic sequestering of protein / tubulin deacetylation / actin crosslink formation / complement component C3b binding / blood coagulation, intrinsic pathway / protein localization to bicellular tight junction / OAS antiviral response / neutrophil migration / Toll Like Receptor 4 (TLR4) Cascade / positive regulation of actin filament bundle assembly / negative regulation of dopamine metabolic process / cell-cell adhesion via plasma-membrane adhesion molecules / positive regulation of neuron migration / positive regulation of potassium ion transmembrane transport / Cell-extracellular matrix interactions / early endosome to late endosome transport / apical dendrite / Fc-gamma receptor I complex binding / cell-cell junction organization / positive regulation of neural precursor cell proliferation / positive regulation of platelet activation / protein localization to cell surface / heterotypic cell-cell adhesion / integrin complex / positive regulation of leukocyte adhesion to vascular endothelial cell / wound healing, spreading of cells / negative regulation of transcription by RNA polymerase I / megakaryocyte development / cell adhesion mediated by integrin / leukocyte cell-cell adhesion / GP1b-IX-V activation signalling / phagocytosis, engulfment / cortical cytoskeleton / positive regulation of axon regeneration / amyloid-beta clearance / endodermal cell differentiation / receptor clustering / SMAD binding / plasma membrane raft / RHO GTPases activate PAKs / actin filament bundle / brush border / tertiary granule membrane / semaphorin-plexin signaling pathway / ficolin-1-rich granule membrane / cellular response to low-density lipoprotein particle stimulus / mitotic spindle assembly / cilium assembly / potassium channel regulator activity / positive regulation of protein targeting to membrane / epithelial to mesenchymal transition / blood vessel remodeling / Integrin cell surface interactions / specific granule membrane / axonal growth cone / heart morphogenesis / positive regulation of substrate adhesion-dependent cell spreading / regulation of peptidyl-tyrosine phosphorylation / release of sequestered calcium ion into cytosol / regulation of cell migration / cell adhesion molecule binding / heat shock protein binding / neutrophil chemotaxis / cell-matrix adhesion / receptor-mediated endocytosis / positive regulation of superoxide anion generation / dendritic shaft / protein localization to plasma membrane / G protein-coupled receptor binding / integrin-mediated signaling pathway / actin filament / Cell surface interactions at the vascular wall / protein kinase C binding / synapse organization / microglial cell activation / mRNA transcription by RNA polymerase II / establishment of protein localization / trans-Golgi network / negative regulation of protein catabolic process / negative regulation of DNA-binding transcription factor activity / receptor internalization / cerebral cortex development / small GTPase binding / kinase binding / platelet aggregation / Z disc
Similarity search - Function
Integrin beta-2 subunit / Filamin family / Filamin/ABP280 repeat / Filamin-type immunoglobulin domains / Filamin/ABP280 repeat / Filamin/ABP280 repeat profile. / Filamin/ABP280 repeat-like / Integrin beta subunit, cytoplasmic domain / Integrin beta cytoplasmic domain / Integrin_b_cyt ...Integrin beta-2 subunit / Filamin family / Filamin/ABP280 repeat / Filamin-type immunoglobulin domains / Filamin/ABP280 repeat / Filamin/ABP280 repeat profile. / Filamin/ABP280 repeat-like / Integrin beta subunit, cytoplasmic domain / Integrin beta cytoplasmic domain / Integrin_b_cyt / Integrin beta tail domain / Integrin beta subunit, tail / Integrin beta tail domain superfamily / Integrin_B_tail / Integrin beta subunit, VWA domain / Integrin beta subunit / Integrin beta N-terminal / Integrin beta chain VWA domain / Integrin plexin domain / Integrins beta chain cysteine-rich domain signature. / Integrin beta subunits (N-terminal portion of extracellular region) / Actinin-type actin-binding domain signature 1. / Actinin-type actin-binding domain signature 2. / Actinin-type actin-binding domain, conserved site / Integrin domain superfamily / Calponin homology domain / Calponin homology (CH) domain / PSI domain / domain found in Plexins, Semaphorins and Integrins / Calponin homology domain / CH domain superfamily / Calponin homology (CH) domain profile. / von Willebrand factor A-like domain superfamily / EGF-like domain signature 2. / EGF-like domain signature 1. / Immunoglobulin E-set / Immunoglobulins / Immunoglobulin-like fold / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Integrin beta-2 / Filamin-A
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / torsion angle dynamics
AuthorsChatterjee, D. / Lu, L.Z. / Bhattacharjya, S.
Funding support Singapore, 1items
OrganizationGrant numberCountry
Ministry of EducationARC18/13 Singapore
CitationJournal: To Be Published
Title: Structure of FLN IG21 domain in complex with C-terminal peptide of beta-2
Authors: Chatterjee, D. / Lu, L.Z. / Bhattachrjya, S.
History
DepositionJun 7, 2017Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jun 13, 2018Provider: repository / Type: Initial release
Revision 1.1Jun 14, 2023Group: Data collection / Database references / Other
Category: database_2 / pdbx_database_status / pdbx_nmr_spectrometer
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data / _pdbx_nmr_spectrometer.model
Revision 1.2May 15, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 / Item: _database_2.pdbx_DOI

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: C-terminal peptide of Integrin beta-2,Filamin-A IG21 domain


Theoretical massNumber of molelcules
Total (without water)13,7571
Polymers13,7571
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: native gel electrophoresis, gel filtration
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area0 Å2
ΔGint0 kcal/mol
Surface area5970 Å2
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 200structures with the lowest energy
RepresentativeModel #1lowest energy

-
Components

#1: Protein C-terminal peptide of Integrin beta-2,Filamin-A IG21 domain / Cell surface adhesion glycoproteins LFA-1/CR3/p150 / 95 subunit beta / Complement receptor C3 ...Cell surface adhesion glycoproteins LFA-1/CR3/p150 / 95 subunit beta / Complement receptor C3 subunit beta / FLN-A / Actin-binding protein 280 / ABP-280 / Alpha-filamin / Endothelial actin-binding protein / Filamin-1 / Non-muscle filamin


Mass: 13757.035 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: Fusion protein of C-terminal peptide of Integrin beta-2 (residues 752-763, P05107 (ITB2_HUMAN)), and Filamin-A IG21 domain (residues 2228-2321, P21333 (FLNA_HUMAN)).
Source: (gene. exp.) Homo sapiens (human) / Gene: ITGB2, CD18, MFI7, FLNA, FLN, FLN1
Production host: BAC cloning vector attB-P[acman]-ApR-F-2-5-attB (others)
References: UniProt: P05107, UniProt: P21333

-
Experimental details

-
Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDSample stateSpectrometer-IDType
111isotropic12D 1H-15N HSQC
121isotropic13D CBCA(CO)NH
131isotropic13D HN(CA)CB
141isotropic13D 1H-15N NOESY
151isotropic13D 1H-13C NOESY
161isotropic13D 1H-15N TOCSY

-
Sample preparation

DetailsType: solution
Contents: 300 uM [U-13C; U-15N] FLN IG21 domain, 90% H2O/10% D2O
Label: 15N, 13C_ / Solvent system: 90% H2O/10% D2O
SampleConc.: 300 uM / Component: FLN IG21 domain / Isotopic labeling: [U-13C; U-15N]
Sample conditionsIonic strength: 150 mM / Label: Uniformaly 13C, 15N labeled / pH: 6.2 / Pressure: 1 atm / Temperature: 298 K

-
NMR measurement

NMR spectrometerType: Bruker AVANCE III / Manufacturer: Bruker / Model: AVANCE III / Field strength: 600 MHz

-
Processing

NMR softwareName: CNS / Developer: Brunger A. T. et.al. / Classification: refinement
RefinementMethod: torsion angle dynamics / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 200 / Conformers submitted total number: 20

+
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://pdbjlvh1.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