[English] 日本語
Yorodumi
- PDB-6u4n: Solution structure of paxillin LIM4 in complex with kindlin-2 F0 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 6u4n
TitleSolution structure of paxillin LIM4 in complex with kindlin-2 F0
Components
  • Fermitin family homolog 2
  • Paxillin
KeywordsCELL ADHESION / LIM domain / Zinc finger / Ubiquitin fold / Complex
Function / homology
Function and homology information


adherens junction maintenance / Localization of the PINCH-ILK-PARVIN complex to focal adhesions / Regulation of cytoskeletal remodeling and cell spreading by IPP complex components / positive regulation of myosin light chain kinase activity / protein localization to cell junction / positive regulation of mesenchymal stem cell proliferation / positive regulation of wound healing, spreading of epidermal cells / vinculin binding / positive regulation of integrin activation / Cell-extracellular matrix interactions ...adherens junction maintenance / Localization of the PINCH-ILK-PARVIN complex to focal adhesions / Regulation of cytoskeletal remodeling and cell spreading by IPP complex components / positive regulation of myosin light chain kinase activity / protein localization to cell junction / positive regulation of mesenchymal stem cell proliferation / positive regulation of wound healing, spreading of epidermal cells / vinculin binding / positive regulation of integrin activation / Cell-extracellular matrix interactions / type I transforming growth factor beta receptor binding / neuropilin binding / integrin activation / focal adhesion assembly / signal complex assembly / protein localization to membrane / negative regulation of vascular permeability / regulation of cell morphogenesis / I band / limb development / microtubule associated complex / growth hormone receptor signaling pathway / negative regulation of fat cell differentiation / SMAD binding / phosphatidylinositol-3,4,5-trisphosphate binding / positive regulation of focal adhesion assembly / lamellipodium membrane / endothelial cell migration / Smooth Muscle Contraction / positive regulation of epithelial to mesenchymal transition / RAC3 GTPase cycle / positive regulation of osteoblast differentiation / GAB1 signalosome / PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases / positive regulation of substrate adhesion-dependent cell spreading / stress fiber / positive regulation of stress fiber assembly / RAC1 GTPase cycle / extrinsic component of cytoplasmic side of plasma membrane / substrate adhesion-dependent cell spreading / cell-matrix adhesion / transforming growth factor beta receptor signaling pathway / integrin-mediated signaling pathway / adherens junction / cytoplasmic side of plasma membrane / beta-catenin binding / Wnt signaling pathway / cellular response to reactive oxygen species / positive regulation of GTPase activity / VEGFA-VEGFR2 Pathway / positive regulation of protein localization to nucleus / actin filament binding / cell-cell junction / cell migration / integrin binding / lamellipodium / cell junction / actin binding / cell cortex / regulation of cell shape / protein phosphatase binding / positive regulation of ERK1 and ERK2 cascade / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / cell adhesion / positive regulation of cell migration / focal adhesion / protein kinase binding / cell surface / signal transduction / nucleoplasm / metal ion binding / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Kindlin/fermitin, PH domain / Kindlin/fermitin / Kindlin-2, N-terminal / Kindlin-2 N-terminal domain / Paxillin / : / : / Paxillin family / Cysteine Rich Protein / Cysteine Rich Protein ...Kindlin/fermitin, PH domain / Kindlin/fermitin / Kindlin-2, N-terminal / Kindlin-2 N-terminal domain / Paxillin / : / : / Paxillin family / Cysteine Rich Protein / Cysteine Rich Protein / LIM zinc-binding domain signature. / LIM domain / Zinc-binding domain present in Lin-11, Isl-1, Mec-3. / Zinc finger, LIM-type / LIM domain profile. / FERM central domain / FERM central domain / FERM superfamily, second domain / Band 4.1 domain / Band 4.1 homologues / PH domain / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / PH domain profile. / Pleckstrin homology domain. / Pleckstrin homology domain / Ubiquitin-like (UB roll) / Ribbon / PH-like domain superfamily / Roll / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Paxillin / Fermitin family homolog 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing
AuthorsZhu, L. / Qin, J.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Human Genome Research Institute (NIH/NHGRI) United States
CitationJournal: Structure / Year: 2019
Title: Structural Basis of Paxillin Recruitment by Kindlin-2 in Regulating Cell Adhesion.
Authors: Zhu, L. / Liu, H. / Lu, F. / Yang, J. / Byzova, T.V. / Qin, J.
History
DepositionAug 26, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 23, 2019Provider: repository / Type: Initial release
Revision 1.1Nov 20, 2019Group: Database references / Category: citation / Item: _citation.journal_volume / _citation.page_first
Revision 1.2Dec 18, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Fermitin family homolog 2
B: Paxillin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)21,4434
Polymers21,3122
Non-polymers1312
Water0
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: surface plasmon resonance
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area1060 Å2
ΔGint-9 kcal/mol
Surface area10660 Å2
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 100structures with the lowest energy
RepresentativeModel #1lowest energy

-
Components

#1: Protein Fermitin family homolog 2 / Kindlin-2 / Mitogen-inducible gene 2 protein / MIG-2 / Pleckstrin homology domain-containing family ...Kindlin-2 / Mitogen-inducible gene 2 protein / MIG-2 / Pleckstrin homology domain-containing family C member 1 / PH domain-containing family C member 1


Mass: 13002.017 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FERMT2, KIND2, MIG2, PLEKHC1 / Plasmid: pGST-1 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q96AC1
#2: Protein Paxillin /


Mass: 8309.760 Da / Num. of mol.: 1 / Fragment: LIM4 domain residues 527-591
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PXN / Plasmid: pGST-1 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P49023
#3: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
Has ligand of interestN

-
Experimental details

-
Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDSample stateSpectrometer-IDType
111isotropic13D 15N/13C-edited NOESY
122isotropic13D 15N/13C-edited NOESY
233isotropic13D 15N/13C-filtered NOESY
244isotropic13D 15N/13C-filtered NOESY

-
Sample preparation

Details
TypeSolution-IDContentsDetailsLabelSolvent system
solution10.55 mM U-15N, U-13C paxillin LIM4, 0.89 mM kindlin-2 F0, 95% H2O/5% D2O0.55 mM 15N/13C-labeled paxillin LIM4 in the presence of 0.89 mM unlabeled kindlin-2 F015N, 13C_195% H2O/5% D2O
solution20.54 mM U-15N, U-13C kindlin-2 F0, 0.85 mM paxillin LIM4, 95% H2O/5% D2O0.54 mM 15N/13C- labeled kindlin-2 F0 in the presence of 0.85 mM unlabeled paxillin LIM415N, 13C_295% H2O/5% D2O
solution30.55 mM U-15N, U-13C paxillin LIM4, 0.89 mM kindlin-2 F0, 99.8% D2O0.55 mM 15N/13C-labeled paxillin LIM4 in the presence of 0.89 mM unlabeled kindlin-2 F0 prepared in 99.8% D2O15N, 13C_399.8% D2O
solution40.54 mM U-15N, U-13C kindlin-2 F0, 0.85 mM paxillin LIM4, 99.8% D2O0.54 mM 15N/13C- labeled kindlin-2 F0 in the presence of 0.85 mM unlabeled paxillin LIM4 prepared in 99.8% D2O15N, 13C_499.8% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
0.55 mMpaxillin LIM4U-15N, U-13C1
0.89 mMkindlin-2 F0natural abundance1
0.54 mMkindlin-2 F0U-15N, U-13C2
0.85 mMpaxillin LIM4natural abundance2
0.55 mMpaxillin LIM4U-15N, U-13C3
0.89 mMkindlin-2 F0natural abundance3
0.54 mMkindlin-2 F0U-15N, U-13C4
0.85 mMpaxillin LIM4natural abundance4
Sample conditions
Conditions-IDDetailsIonic strengthLabelpHPressure (kPa)Temperature (K)
150 mM NaH2PO4/Na2HPO4 (pH 6.8), 50 mM NaCl, 0.5 mM TCEP and 5% D2O50 mM NaCl mMconditions_16.8 ambient Pa298 K
250 mM NaH2PO4/Na2HPO4 (pH 6.8), 50 mM NaCl, 0.5 mM TCEP in 99.8% D2O50 mM NaCl mMconditions_26.8 ambient Pa298 K

-
NMR measurement

NMR spectrometerType: Bruker AVANCE III / Manufacturer: Bruker / Model: AVANCE III / Field strength: 850 MHz

-
Processing

NMR software
NameDeveloperClassification
X-PLOR NIHSchwieters, Kuszewski, Tjandra and Clorestructure calculation
X-PLOR NIHSchwieters, Kuszewski, Tjandra and Clorerefinement
NMRPipeDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Baxdata analysis
PIPPGarrettpeak picking
TALOSCornilescu, Delaglio and Baxdata analysis
RefinementMethod: simulated annealing / Software ordinal: 2
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 100 / 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://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