PDBsum entry 1u6h

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protein Protein-protein interface(s) links
Cell adhesion PDB id
Protein chains
252 a.a. *
24 a.a. *
Waters ×57
* Residue conservation analysis
PDB id:
Name: Cell adhesion
Title: Vinculin head (0-258) in complex with the talin vinculin binding site 2 (849-879)
Structure: Vinculin. Chain: a. Fragment: residues 0-258. Engineered: yes. Talin. Chain: b. Fragment: vinculin binding site 2 (residues 849-879). Engineered: yes
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Gene: vcl, vinc1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Other_details: the peptide was chemically synthesized. The sequence of the peptide is naturally found in gallus
Biol. unit: Dimer (from PQS)
2.38Å     R-factor:   0.246     R-free:   0.322
Authors: I.Fillingham,A.R.Gingras,E.Papagrigoriou,B.Patel,J.Emsley, G.C.K.Roberts,D.R.Critchley,I.L.Barsukov
Key ref:
I.Fillingham et al. (2005). A vinculin binding domain from the talin rod unfolds to form a complex with the vinculin head. Structure, 13, 65-74. PubMed id: 15642262 DOI: 10.1016/j.str.2004.11.006
30-Jul-04     Release date:   18-Jan-05    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P12003  (VINC_CHICK) -  Vinculin
1135 a.a.
252 a.a.
Protein chain
Pfam   ArchSchema ?
P54939  (TLN1_CHICK) -  Talin-1
2541 a.a.
24 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     actin cytoskeleton   1 term 
  Biological process     cell adhesion   1 term 
  Biochemical function     structural molecule activity     1 term  


DOI no: 10.1016/j.str.2004.11.006 Structure 13:65-74 (2005)
PubMed id: 15642262  
A vinculin binding domain from the talin rod unfolds to form a complex with the vinculin head.
I.Fillingham, A.R.Gingras, E.Papagrigoriou, B.Patel, J.Emsley, D.R.Critchley, G.C.Roberts, I.L.Barsukov.
The cytoskeletal protein talin plays a key role in activating integrins and in coupling them to the actin cytoskeleton. Its N-terminal globular head, which binds beta integrins, is linked to an extended rod having a C-terminal actin binding site and several vinculin binding sites (VBSs). The NMR structure of residues 755-889 of the rod (containing a VBS) is shown to be an amphipathic four-helix bundle with a left-handed topology. A talin peptide corresponding to the VBS binds the vinculin head; the X-ray crystallographic structure of this complex shows that the residues which interact with vinculin are buried in the hydrophobic core of the talin fragment. NMR shows that the interaction involves a major structural change in the talin fragment, including unfolding of one of its helices, making the VBS accessible to vinculin. Interestingly, the talin 755-889 fragment binds more than one vinculin head molecule, suggesting that the talin rod may contain additional as yet unrecognized VBSs.
  Selected figure(s)  
Figure 1.
Figure 1. Solution Structure of Talin 755-889
(A) Stereo view of the superposition (using backbone atoms in the helices) of the 20 lowest energy structures consistent with the NMR data. Only the structural core region (residues 763-878) is shown, not the disordered N and C termini.
(B) Stereo view of a representative low energy structure showing the residues comprising the hydrophobic clusters and the "threonine belt"--see text.
(C) Representations of the NMR structure of talin 755-889 (left) and the X-ray structure of talin 656-789 (right). The order of the helices from the N to the C terminus is represented by the color, in the order red, green, blue, and purple. Talin 755-889 has the same orientation in (A)-(C).
(D) The sequence of talin 755-889 indicating the positions of the a helices, corresponding to the colors in (C).
  The above figure is reprinted by permission from Cell Press: Structure (2005, 13, 65-74) copyright 2005.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20610383 A.R.Gingras, N.Bate, B.T.Goult, B.Patel, P.M.Kopp, J.Emsley, I.L.Barsukov, G.C.Roberts, and D.R.Critchley (2010).
Central region of talin has a unique fold that binds vinculin and actin.
  J Biol Chem, 285, 29577-29587.
PDB code: 2x0c
20399778 B.T.Goult, A.R.Gingras, N.Bate, I.L.Barsukov, D.R.Critchley, and G.C.Roberts (2010).
The domain structure of talin: residues 1815-1973 form a five-helix bundle containing a cryptic vinculin-binding site.
  FEBS Lett, 584, 2237-2241.
PDB code: 2kvp
19179532 A.del Rio, R.Perez-Jimenez, R.Liu, P.Roca-Cusachs, J.M.Fernandez, and M.P.Sheetz (2009).
Stretching single talin rod molecules activates vinculin binding.
  Science, 323, 638-641.  
19297334 B.T.Goult, N.Bate, N.J.Anthis, K.L.Wegener, A.R.Gingras, B.Patel, I.L.Barsukov, I.D.Campbell, G.C.Roberts, and D.R.Critchley (2009).
The structure of an interdomain complex that regulates talin activity.
  J Biol Chem, 284, 15097-15106.
PDB codes: 2kbb 2kgx
19416068 D.R.Critchley (2009).
Biochemical and structural properties of the integrin-associated cytoskeletal protein talin.
  Annu Rev Biophys, 38, 235-254.  
19655048 G.C.Roberts, and D.R.Critchley (2009).
Structural and biophysical properties of the integrin-associated cytoskeletal protein talin.
  Biophys Rev, 1, 61-69.  
19598236 H.Wolfenson, Y.I.Henis, B.Geiger, and A.D.Bershadsky (2009).
The heel and toe of the cell's foot: a multifaceted approach for understanding the structure and dynamics of focal adhesions.
  Cell Motil Cytoskeleton, 66, 1017-1029.  
19523901 J.H.Lee, E.S.Rangarajan, S.D.Yogesha, and T.Izard (2009).
Raver1 interactions with vinculin and RNA suggest a feed-forward pathway in directing mRNA to focal adhesions.
  Structure, 17, 833-842.
PDB codes: 3h2u 3h2v
19217273 V.Vogel, and M.P.Sheetz (2009).
Cell fate regulation by coupling mechanical cycles to biochemical signaling pathways.
  Curr Opin Cell Biol, 21, 38-46.  
18157087 A.R.Gingras, N.Bate, B.T.Goult, L.Hazelwood, I.Canestrelli, J.G.Grossmann, H.Liu, N.S.Putz, G.C.Roberts, N.Volkmann, D.Hanein, I.L.Barsukov, and D.R.Critchley (2008).
The structure of the C-terminal actin-binding domain of talin.
  EMBO J, 27, 458-469.
PDB codes: 2jsw 2qdq
18614051 E.Goksoy, Y.Q.Ma, X.Wang, X.Kong, D.Perera, E.F.Plow, and J.Qin (2008).
Structural basis for the autoinhibition of talin in regulating integrin activation.
  Mol Cell, 31, 124-133.  
18577523 S.Rodius, O.Chaloin, M.Moes, E.Schaffner-Reckinger, I.Landrieu, G.Lippens, M.Lin, J.Zhang, and N.Kieffer (2008).
The Talin Rod IBS2 {alpha}-Helix Interacts with the {beta}3 Integrin Cytoplasmic Tail Membrane-proximal Helix by Establishing Charge Complementary Salt Bridges.
  J Biol Chem, 283, 24212-24223.  
18282082 V.P.Hytönen, and V.Vogel (2008).
How force might activate talin's vinculin binding sites: SMD reveals a structural mechanism.
  PLoS Comput Biol, 4, e24.  
18186487 Y.G.Gao, M.Yao, and I.Tanaka (2008).
Structure of protein PH0536 from Pyrococcus horikoshii at 1.7 A resolution reveals a novel assembly of an oligonucleotide/oligosaccharide-binding fold and an alpha-helical bundle.
  Proteins, 71, 503-508.
PDB code: 2e8g
17932491 G.T.Nhieu, and T.Izard (2007).
Vinculin binding in its closed conformation by a helix addition mechanism.
  EMBO J, 26, 4588-4596.
PDB code: 2ibf
17184985 I.Delon, and N.H.Brown (2007).
Integrins and the actin cytoskeleton.
  Curr Opin Cell Biol, 19, 43-50.  
18056416 J.D.Humphries, P.Wang, C.Streuli, B.Geiger, M.J.Humphries, and C.Ballestrem (2007).
Vinculin controls focal adhesion formation by direct interactions with talin and actin.
  J Cell Biol, 179, 1043-1057.  
17928215 M.A.Arnaout, S.L.Goodman, and J.P.Xiong (2007).
Structure and mechanics of integrin-based cell adhesion.
  Curr Opin Cell Biol, 19, 495-507.  
17430904 M.Moes, S.Rodius, S.J.Coleman, S.J.Monkley, E.Goormaghtigh, L.Tremuth, C.Kox, P.P.van der Holst, D.R.Critchley, and N.Kieffer (2007).
The integrin binding site 2 (IBS2) in the talin rod domain is essential for linking integrin beta subunits to the cytoskeleton.
  J Biol Chem, 282, 17280-17288.  
16407302 B.Patel, A.R.Gingras, A.A.Bobkov, L.M.Fujimoto, M.Zhang, R.C.Liddington, D.Mazzeo, J.Emsley, G.C.Roberts, I.L.Barsukov, and D.R.Critchley (2006).
The activity of the vinculin binding sites in talin is influenced by the stability of the helical bundles that make up the talin rod.
  J Biol Chem, 281, 7458-7467.  
16826238 C.Hamiaux, A.van Eerde, C.Parsot, J.Broos, and B.W.Dijkstra (2006).
Structural mimicry for vinculin activation by IpaA, a virulence factor of Shigella flexneri.
  EMBO Rep, 7, 794-799.
PDB code: 2gdc
16608855 D.M.Cohen, B.Kutscher, H.Chen, D.B.Murphy, and S.W.Craig (2006).
A conformational switch in vinculin drives formation and dynamics of a talin-vinculin complex at focal adhesions.
  J Biol Chem, 281, 16006-16015.  
16460282 J.J.Fredberg, and R.D.Kamm (2006).
Stress transmission in the lung: pathways from organ to molecule.
  Annu Rev Physiol, 68, 507-541.  
16407299 P.R.Bois, B.P.O'Hara, D.Nietlispach, J.Kirkpatrick, and T.Izard (2006).
The vinculin binding sites of talin and alpha-actinin are sufficient to activate vinculin.
  J Biol Chem, 281, 7228-7236.  
17088427 T.Izard, G.Tran Van Nhieu, and P.R.Bois (2006).
Shigella applies molecular mimicry to subvert vinculin and invade host cells.
  J Cell Biol, 175, 465-475.
PDB codes: 2gww 2hsq
16893648 W.H.Ziegler, R.C.Liddington, and D.R.Critchley (2006).
The structure and regulation of vinculin.
  Trends Cell Biol, 16, 453-460.  
16135522 A.R.Gingras, W.H.Ziegler, R.Frank, I.L.Barsukov, G.C.Roberts, D.R.Critchley, and J.Emsley (2005).
Mapping and consensus sequence identification for multiple vinculin binding sites within the talin rod.
  J Biol Chem, 280, 37217-37224.
PDB codes: 1zvz 1zw2 1zw3
16109371 O.Hantschel, S.Wiesner, T.Güttler, C.D.Mackereth, L.L.Rix, Z.Mikes, J.Dehne, D.Görlich, M.Sattler, and G.Superti-Furga (2005).
Structural basis for the cytoskeletal association of Bcr-Abl/c-Abl.
  Mol Cell, 19, 461-473.
PDB code: 1zzp
15988023 P.R.Bois, R.A.Borgon, C.Vonrhein, and T.Izard (2005).
Structural dynamics of alpha-actinin-vinculin interactions.
  Mol Cell Biol, 25, 6112-6122.
PDB code: 1ydi
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.