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- PDB-2kgx: HADDOCK structure of the talin F3 domain in complex with talin 16... -

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Basic information

Entry
Database: PDB / ID: 2kgx
TitleHADDOCK structure of the talin F3 domain in complex with talin 1655-1822
Components
  • MKIAA1027 protein
  • Talin-1
KeywordsCELL ADHESION / talin / interdomain / F3 / cytoskeleton / Cell membrane / Cell projection / Cytoplasm / Membrane / Phosphoprotein
Function / homology
Function and homology information


GRB2:SOS provides linkage to MAPK signaling for Integrins / Integrin signaling / Smooth Muscle Contraction / p130Cas linkage to MAPK signaling for integrins / SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion / MAP2K and MAPK activation / LIM domain binding / Platelet degranulation / vinculin binding / integrin activation ...GRB2:SOS provides linkage to MAPK signaling for Integrins / Integrin signaling / Smooth Muscle Contraction / p130Cas linkage to MAPK signaling for integrins / SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion / MAP2K and MAPK activation / LIM domain binding / Platelet degranulation / vinculin binding / integrin activation / cell-substrate junction assembly / cortical actin cytoskeleton organization / phosphatidylserine binding / ruffle / phosphatidylinositol binding / integrin-mediated signaling pathway / adherens junction / structural constituent of cytoskeleton / platelet aggregation / ruffle membrane / cell-cell adhesion / actin filament binding / integrin binding / cytoskeleton / focal adhesion / cell surface / plasma membrane / cytoplasm
Similarity search - Function
Talin, central domain / A middle domain of Talin 1 / : / Talin, R4 domain / Vinculin-binding site-containing domain / Talin, central / Talin, N-terminal F0 domain / Talin, central domain superfamily / Talin-1/2, rod-segment / Vinculin Binding Site ...Talin, central domain / A middle domain of Talin 1 / : / Talin, R4 domain / Vinculin-binding site-containing domain / Talin, central / Talin, N-terminal F0 domain / Talin, central domain superfamily / Talin-1/2, rod-segment / Vinculin Binding Site / Talin, middle domain / N-terminal or F0 domain of Talin-head FERM / I/LWEQ domain / I/LWEQ domain superfamily / I/LWEQ domain / I/LWEQ domain profile. / I/LWEQ domain / Phosphotyrosine-binding domain / Alpha-catenin/vinculin-like superfamily / FERM domain signature 1. / FERM conserved site / FERM domain signature 2. / FERM central domain / FERM/acyl-CoA-binding protein superfamily / Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) / PH-domain like / FERM central domain / FERM superfamily, second domain / FERM domain / FERM domain profile. / Band 4.1 domain / Band 4.1 homologues / PH-like domain superfamily / Ubiquitin-like domain superfamily / Roll / Up-down Bundle / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
Talin-1 / MKIAA1027 protein
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodSOLUTION NMR / Protein-protein docking
AuthorsGoult, B.T. / Gingras, A.R. / Bate, N. / Critchley, D.R. / Barsukov, I.L.
CitationJournal: J.Biol.Chem. / Year: 2009
Title: The structure of an interdomain complex that regulates talin activity.
Authors: Goult, B.T. / Bate, N. / Anthis, N.J. / Wegener, K.L. / Gingras, A.R. / Patel, B. / Barsukov, I.L. / Campbell, I.D. / Roberts, G.C. / Critchley, D.R.
History
DepositionMar 23, 2009Deposition site: BMRB / Processing site: RCSB
Revision 1.0Mar 31, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Oct 20, 2021Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly ...database_2 / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 1.3May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Talin-1
B: MKIAA1027 protein


Theoretical massNumber of molelcules
Total (without water)28,7382
Polymers28,7382
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)2 / 200structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein Talin-1


Mass: 18247.406 Da / Num. of mol.: 1 / Mutation: C336S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Tln1, Tln / Plasmid: pet151 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: P26039
#2: Protein MKIAA1027 protein


Mass: 10490.108 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Tln1, mKIAA1027 / Plasmid: pet151 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: Q80TM2, UniProt: P26039*PLUS

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-15N HSQC
1222D 1H-15N HSQC
1313D 1H-13C NOESY
1423D 1H-13C NOESY
151F1-filtered, F3-edited NOESY
162F1-filtered, F3-edited NOESY

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Sample preparation

Details
Solution-IDContentsSolvent system
10.5 mM [U-100% 15N] 1655-1822, 2 mM F3, 50 mM sodium chloride, 20 mM sodium phosphate, 2 mM DTT, 90% H2O/10% D2O90% H2O/10% D2O
20.5 mM 1655-1822, 2 mM [U-100% 15N] F3, 50 mM sodium chloride, 20 mM sodium phosphate, 2 mM DTT, 90% H2O/10% D2O90% H2O/10% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
0.5 mM1655-1822[U-100% 15N]1
2 mMF31
50 mMsodium chloride1
20 mMsodium phosphate1
2 mMDTT1
0.5 mM1655-18222
2 mMF3[U-100% 15N]2
50 mMsodium chloride2
20 mMsodium phosphate2
2 mMDTT2
Sample conditionsIonic strength: 50 / pH: 6.5 / Pressure: ambient / Temperature: 298 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DRXBrukerDRX6001
Bruker DRXBrukerDRX8002

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Processing

NMR softwareName: HADDOCK / Version: 2 / Developer: Dominguez, C. et al. / Classification: refinement
RefinementMethod: Protein-protein docking / Software ordinal: 1 / Details: HADDOCK algorithm
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 200 / Conformers submitted total number: 2

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