2KVP

Solution Structure of the R10 Domain of Talin


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

The domain structure of talin: Residues 1815-1973 form a five-helix bundle containing a cryptic vinculin-binding site.

Goult, B.T.Gingras, A.R.Bate, N.Barsukov, I.L.Critchley, D.R.Roberts, G.C.

(2010) FEBS Lett 584: 2237-2241

  • DOI: https://doi.org/10.1016/j.febslet.2010.04.028
  • Primary Citation of Related Structures:  
    2KVP

  • PubMed Abstract: 

    Talin is a large flexible rod-shaped protein that activates the integrin family of cell adhesion molecules and couples them to cytoskeletal actin. Its rod region consists of a series of helical bundles. Here we show that residues 1815-1973 form a 5-helix bundle, with a topology unique to talin which is optimally suited for formation of a long rod such as talin. This is much more stable than the 4-helix (1843-1973) domain described earlier and as a result its vinculin binding sequence is inaccessible to vinculin at room temperature, with implications for the overall mechanism of the talin-vinculin interaction.


  • Organizational Affiliation

    Department of Biochemistry, University of Leicester, Leicester, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Talin-1165Mus musculusMutation(s): 0 
Gene Names: TlnTln1
UniProt
Find proteins for P26039 (Mus musculus)
Explore P26039 
Go to UniProtKB:  P26039
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP26039
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the lowest energy 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-05-05
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2021-08-25
    Changes: Data collection, Database references, Derived calculations, Structure summary
  • Version 1.3: 2024-05-22
    Changes: Data collection