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PDBsum entry 2kbb
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Structural protein PDB id
2kbb

 

 

 

 

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Contents
Protein chain
174 a.a. *
* Residue conservation analysis
PDB id:
2kbb
Name: Structural protein
Title: Solution structure of the r9 domain of talin
Structure: Talin-1. Chain: a. Fragment: residues 1655-1822. Engineered: yes
Source: Mus musculus. Mouse. Organism_taxid: 10090. Gene: tln, tln1. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 20 models
Authors: B.T.Goult,A.R.Gingras,N.Bate,D.R.Critchley,I.L.Barsukov
Key ref:
B.T.Goult et al. (2009). The structure of an interdomain complex which regulates talin activity. J Biol Chem, 284, 15097-15106. PubMed id: 19297334 DOI: 10.1074/jbc.M900078200
Date:
24-Nov-08     Release date:   17-Mar-09    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P26039  (TLN1_MOUSE) -  Talin-1 from Mus musculus
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		2541 a.a.
174 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 6 residue positions (black crosses)

 

 
DOI no: 10.1074/jbc.M900078200 J Biol Chem 284:15097-15106 (2009)
PubMed id: 19297334  
 
 
The structure of an interdomain complex which regulates talin activity.
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, D.R.Critchley.
 
  ABSTRACT  
 
Talin is a large flexible rod-shaped protein that activates the integrin family of cell adhesion molecules and couples them to cytoskeletal actin. It exists in both globular and extended conformations, and an intra-molecular interaction between the N-terminal F3 FERM sub-domain and the C-terminal part of the talin rod contributes to an autoinhibited form of the molecule. Here, we report the solution structure of the primary F3 binding domain within the C-terminal region of the talin rod and use intermolecular NOEs to determine the structure of the complex. The rod domain (residues 1655-1822) is an amphipathic 5-helix bundle - Y377 of F3 docks into a hydrophobic pocket at one end of the bundle whilst a basic loop in F3 (residues 316 to 326) interacts with a cluster of acidic residues in the middle of helix 4. Mutation of E1770 abolishes binding. The rod domain competes with beta3-integrin tails for binding to F3 and the structure of the complex suggests that the rod is also likely to sterically inhibit binding of the FERM domain to the membrane.
 
  Selected figure(s)  
 
Figure 1.
Structure of the talin 1655–1822 rod domain. A, schematic representation of the domain structure of talin indicating the relative position of the ligand binding sites and the boundaries of the various head and rod domains. B, sequence alignment of human talin1 residues 1655–1822 with the corresponding regions of other talins. C, superimposition of the 20 lowest energy structures consistent with the NMR data. Only the structured region of 1655–1822 is shown, not the disordered N terminus. D, ribbon drawing of a representative low energy structure showing the overall topology of the five-helix bundle. E, map of the surface charge of the domain. 		Figure 3.
Structure of the complex between talin F3 and talin 1655–1822. A, ribbon representation of the model of talin F3 (red) in complex with talin 1655–1822 (pale blue) obtained using the HADDOCK approach. B, close-up of the interface showing Tyr-377 of F3 and its close proximity to Leu-1680, Val-1683, Met-1759, and Leu-1762 of talin 1655–1822. C, close-up of the interaction of the positively charged activation loop of F3 with the negatively charged residues on talin 1655–1822.
 
  The above figures are reprinted from an Open Access publication published by the ASBMB: J Biol Chem (2009, 284, 15097-15106) copyright 2009.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21216149 N.J.Anthis, and I.D.Campbell (2011).
The tail of integrin activation.
  Trends Biochem Sci, 36, 191-198.  
21087420 P.Pinon, and B.Wehrle-Haller (2011).
Integrins: versatile receptors controlling melanocyte adhesion, migration and proliferation.
  Pigment Cell Melanoma Res, 24, 282-294.  
21081121 S.J.Monkley, V.Kostourou, L.Spence, B.Petrich, S.Coleman, M.H.Ginsberg, C.A.Pritchard, and D.R.Critchley (2011).
Endothelial cell talin1 is essential for embryonic angiogenesis.
  Dev Biol, 349, 494-502.  
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
20665668 J.Lim, A.G.Dupuy, D.R.Critchley, and E.Caron (2010).
Rap1 controls activation of the α(M)β(2) integrin in a talin-dependent manner.
  J Cell Biochem, 111, 999.  
20605055 P.M.Kopp, N.Bate, T.M.Hansen, N.P.Brindle, U.Praekelt, E.Debrand, S.Coleman, D.Mazzeo, B.T.Goult, A.R.Gingras, C.A.Pritchard, D.R.Critchley, and S.J.Monkley (2010).
Studies on the morphology and spreading of human endothelial cells define key inter- and intramolecular interactions for talin1.
  Eur J Cell Biol, 89, 661-673.  
20947018 P.R.Elliott, B.T.Goult, P.M.Kopp, N.Bate, J.G.Grossmann, G.C.Roberts, D.R.Critchley, and I.L.Barsukov (2010).
The Structure of the talin head reveals a novel extended conformation of the FERM domain.
  Structure, 18, 1289-1299.
PDB code: 3ivf
19804783 B.T.Goult, M.Bouaouina, D.S.Harburger, N.Bate, B.Patel, N.J.Anthis, I.D.Campbell, D.A.Calderwood, I.L.Barsukov, G.C.Roberts, and D.R.Critchley (2009).
The structure of the N-terminus of kindlin-1: a domain important for alphaiibbeta3 integrin activation.
  J Mol Biol, 394, 944-956.
PDB code: 2kmc
19553810 E.F.Plow, J.Qin, and T.Byzova (2009).
Kindling the flame of integrin activation and function with kindlins.
  Curr Opin Hematol, 16, 323-328.  
19948488 F.Saltel, E.Mortier, V.P.Hytönen, M.C.Jacquier, P.Zimmermann, V.Vogel, W.Liu, and B.Wehrle-Haller (2009).
New PI(4,5)P2- and membrane proximal integrin-binding motifs in the talin head control beta3-integrin clustering.
  J Cell Biol, 187, 715-731.  
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.

 

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