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PDBsum entry 3s90

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protein Protein-protein interface(s) links
Cell adhesion PDB id
3s90
Jmol
Contents
Protein chains
248 a.a.
27 a.a.
26 a.a.
Waters ×406
PDB id:
3s90
Name: Cell adhesion
Title: Human vinculin head domain vh1 (residues 1-252) in complex w talin (vbs33; residues 1512-1546)
Structure: Vinculin. Chain: a, b. Fragment: unp residues 1-252. Synonym: metavinculin. Engineered: yes. Talin-1. Chain: c, d. Fragment: unp residues 1512-1546. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: vcl. Expressed in: escherichia coli. Expression_system_taxid: 562. Mus musculus. Mouse. Organism_taxid: 10090.
Resolution:
1.97Å     R-factor:   0.187     R-free:   0.210
Authors: S.D Yogesha,A.Sharff,G.Bricogne,T.Izard
Key ref: S.D.Yogesha et al. (2011). Intermolecular versus intramolecular interactions of the vinculin binding site 33 of talin. Protein Sci, 20, 1471-1476. PubMed id: 21648001 DOI: 10.1002/pro.671
Date:
31-May-11     Release date:   22-Jun-11    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P18206  (VINC_HUMAN) -  Vinculin
Seq:
Struc:
 
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Seq:
Struc:
1134 a.a.
248 a.a.
Protein chain
Pfam   ArchSchema ?
P26039  (TLN1_MOUSE) -  Talin-1
Seq:
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Seq:
Struc:
2541 a.a.
27 a.a.
Protein chain
Pfam   ArchSchema ?
P26039  (TLN1_MOUSE) -  Talin-1
Seq:
Struc:
 
Seq:
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Seq:
Struc:
2541 a.a.
26 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     actin cytoskeleton   1 term 
  Biological process     cell adhesion   2 terms 
  Biochemical function     structural molecule activity     2 terms  

 

 
DOI no: 10.1002/pro.671 Protein Sci 20:1471-1476 (2011)
PubMed id: 21648001  
 
 
Intermolecular versus intramolecular interactions of the vinculin binding site 33 of talin.
S.D.Yogesha, A.Sharff, G.Bricogne, T.Izard.
 
  ABSTRACT  
 
The cytoskeletal proteins talin and vinculin are localized at cell-matrix junctions and are key regulators of cell signaling, adhesion, and migration. Talin couples integrins via its FERM domain to F-actin and is an important regulator of integrin activation and clustering. The 220 kDa talin rod domain comprises several four- and five-helix bundles that harbor amphipathic α-helical vinculin binding sites (VBSs). In its inactive state, the hydrophobic VBS residues involved in binding to vinculin are buried within these helix bundles, and the mechanical force emanating from bound integrin receptors is thought necessary for their release and binding to vinculin. The crystal structure of a four-helix bundle of talin that harbors one of these VBSs, coined VBS33, was recently determined. Here we report the crystal structure of VBS33 in complex with vinculin at 2 Å resolution. Notably, comparison of the apo and vinculin bound structures shows that intermolecular interactions of the VBS33 α-helix with vinculin are more extensive than the intramolecular interactions of the VBS33 within the talin four-helix bundle.