PDBsum entry 1tr2

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protein Protein-protein interface(s) links
Cell adhesion PDB id
Protein chain
1028 a.a. *
Waters ×218
* Residue conservation analysis
PDB id:
Name: Cell adhesion
Title: Crystal structure of human full-length vinculin (residues 1- 1066)
Structure: Vinculin isoform 1. Chain: a, b. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: vcl. Expressed in: escherichia coli. Expression_system_taxid: 562.
2.90Å     R-factor:   0.236     R-free:   0.300
Authors: R.A.Borgon,C.Vonrhein,G.Bricogne,P.R.Bois,T.Izard
Key ref:
R.A.Borgon et al. (2004). Crystal structure of human vinculin. Structure, 12, 1189-1197. PubMed id: 15242595 DOI: 10.1016/j.str.2004.05.009
19-Jun-04     Release date:   15-Nov-05    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P18206  (VINC_HUMAN) -  Vinculin
1134 a.a.
1028 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   18 terms 
  Biological process     epithelial cell-cell adhesion   17 terms 
  Biochemical function     dystroglycan binding     8 terms  


DOI no: 10.1016/j.str.2004.05.009 Structure 12:1189-1197 (2004)
PubMed id: 15242595  
Crystal structure of human vinculin.
R.A.Borgon, C.Vonrhein, G.Bricogne, P.R.Bois, T.Izard.
Alterations in the actin cytoskeleton following the formation of cell-matrix and cell-cell junctions are orchestrated by vinculin. Vinculin associates with a large number of cytoskeletal and signaling proteins, and this flexibility is thought to contribute to rapid dissociation and reassociations of adhesion complexes. Intramolecular interactions between vinculin's head (Vh) and tail (Vt) domains limit access of its binding sites for other adhesion proteins. While the crystal structures of the Vh and Vt domains are known, these domains represent less than half of the entire protein and are separated by a large central region of unknown structure and function. Here we report the crystal structure of human full-length vinculin to 2.85 A resolution. In its resting state, vinculin is a loosely packed collection of alpha-helical bundles held together by Vh-Vt interactions. The three new well ordered alpha-helical bundle domains are similar in their structure to either Vh (Vh2 and Vh3) or to Vt (Vt2) and their loose packing provides the necessary flexibility that allows vinculin to interact with its various protein partners at sites of cell adhesion.
  Selected figure(s)  
Figure 2.
Figure 2. The Structure of the Vh and Vt domains in Full-Length VinculinCa trace superposition of vinculin's head (Vh, yellow) and tail (Vt, light blue) as seen in the Vh:Vt complex structure onto the Vh and Vt domains (gray) as found in the full-length structure in the two monomers in the asymmetric unit, by superposition of the Vt domains. Residues 259-879 corresponding to domains Vh2, Vh3, and Vt2, as seen in the full-length structure, are not shown. Every tenth Ca is labeled.
  The above figure is reprinted by permission from Cell Press: Structure (2004, 12, 1189-1197) copyright 2004.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
23292143 E.S.Rangarajan, and T.Izard (2013).
Dimer asymmetry defines α-catenin interactions.
  Nat Struct Mol Biol, 20, 188-193.
PDB code: 4igg
20689042 A.V.Kwiatkowski, S.L.Maiden, S.Pokutta, H.J.Choi, J.M.Benjamin, A.M.Lynch, W.J.Nelson, W.I.Weis, and J.Hardin (2010).
In vitro and in vivo reconstitution of the cadherin-catenin-actin complex from Caenorhabditis elegans.
  Proc Natl Acad Sci U S A, 107, 14591-14596.  
20502710 E.S.Rangarajan, J.H.Lee, S.D.Yogesha, and T.Izard (2010).
A helix replacement mechanism directs metavinculin functions.
  PLoS One, 5, e10679.
PDB code: 3myi
20233164 W.H.Goldmann (2010).
Correlation between the interaction of the vinculin tail domain with lipid membranes, its phosphorylation and cell mechanical behaviour.
  Cell Biol Int, 34, 339-342.  
  19952892 A.Zemljic-Harpf, A.M.Manso, and R.S.Ross (2009).
Vinculin and talin: focus on the myocardium.
  J Investig Med, 57, 849-855.  
19350419 C.T.Mierke (2009).
The role of vinculin in the regulation of the mechanical properties of cells.
  Cell Biochem Biophys, 53, 115-126.  
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.  
20006947 G.Diez, P.Kollmannsberger, C.T.Mierke, T.M.Koch, H.Vali, B.Fabry, and W.H.Goldmann (2009).
Anchorage of vinculin to lipid membranes influences cell mechanical properties.
  Biophys J, 97, 3105-3112.  
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
19110481 S.M.Palmer, M.P.Playford, S.W.Craig, M.D.Schaller, and S.L.Campbell (2009).
Lipid Binding to the Tail Domain of Vinculin: SPECIFICITY AND THE ROLE OF THE N AND C TERMINI.
  J Biol Chem, 284, 7223-7231.  
17785437 A.E.Zemljic-Harpf, J.C.Miller, S.A.Henderson, A.T.Wright, A.M.Manso, L.Elsherif, N.D.Dalton, A.K.Thor, G.A.Perkins, A.D.McCulloch, and R.S.Ross (2007).
Cardiac-myocyte-specific excision of the vinculin gene disrupts cellular junctions, causing sudden death or dilated cardiomyopathy.
  Mol Cell Biol, 27, 7522-7537.  
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
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.  
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
  16569237 D.L.Scott, G.Diez, and W.H.Goldmann (2006).
Protein-lipid interactions: correlation of a predictive algorithm for lipid-binding sites with three-dimensional structural data.
  Theor Biol Med Model, 3, 17.  
17074767 H.Chen, D.M.Choudhury, and S.W.Craig (2006).
Coincidence of actin filaments and talin is required to activate vinculin.
  J Biol Chem, 281, 40389-40398.  
16427016 M.E.Janssen, E.Kim, H.Liu, L.M.Fujimoto, A.Bobkov, N.Volkmann, and D.Hanein (2006).
Three-dimensional structure of vinculin bound to actin filaments.
  Mol Cell, 21, 271-281.  
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.  
15728584 D.M.Cohen, H.Chen, R.P.Johnson, B.Choudhury, and S.W.Craig (2005).
Two distinct head-tail interfaces cooperate to suppress activation of vinculin by talin.
  J Biol Chem, 280, 17109-17117.  
15883197 H.Chen, D.M.Cohen, D.M.Choudhury, N.Kioka, and S.W.Craig (2005).
Spatial distribution and functional significance of activated vinculin in living cells.
  J Cell Biol, 169, 459-470.  
15795225 K.Briknarová, F.Nasertorabi, M.L.Havert, E.Eggleston, D.W.Hoyt, C.Li, A.J.Olson, K.Vuori, and K.R.Ely (2005).
The serine-rich domain from Crk-associated substrate (p130cas) is a four-helix bundle.
  J Biol Chem, 280, 21908-21914.
PDB code: 1z23
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
15501673 K.A.Demali (2004).
Vinculin--a dynamic regulator of cell adhesion.
  Trends Biochem Sci, 29, 565-567.  
15229287 Z.Zhang, G.Izaguirre, S.Y.Lin, H.Y.Lee, E.Schaefer, and B.Haimovich (2004).
The phosphorylation of vinculin on tyrosine residues 100 and 1065, mediated by SRC kinases, affects cell spreading.
  Mol Biol Cell, 15, 4234-4247.  
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.