PDBsum entry 3myi

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protein links
Cell adhesion PDB id
Protein chain
163 a.a. *
Waters ×93
* Residue conservation analysis
PDB id:
Name: Cell adhesion
Title: Human metavinculin tail domain
Structure: Vinculin. Chain: a. Fragment: unp residues 959-1134. Synonym: metavinculin. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: vcl. Expressed in: escherichia coli. Expression_system_taxid: 562
2.20Å     R-factor:   0.193     R-free:   0.247
Authors: T.Izard,E.S.Rangarajan
Key ref: E.S.Rangarajan et al. (2010). A helix replacement mechanism directs metavinculin functions. PLoS One, 5, e10679. PubMed id: 20502710
10-May-10     Release date:   26-May-10    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P18206  (VINC_HUMAN) -  Vinculin
1134 a.a.
163 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  


PLoS One 5:e10679 (2010)
PubMed id: 20502710  
A helix replacement mechanism directs metavinculin functions.
E.S.Rangarajan, J.H.Lee, S.D.Yogesha, T.Izard.
Cells require distinct adhesion complexes to form contacts with their neighbors or the extracellular matrix, and vinculin links these complexes to the actin cytoskeleton. Metavinculin, an isoform of vinculin that harbors a unique 68-residue insert in its tail domain, has distinct actin bundling and oligomerization properties and plays essential roles in muscle development and homeostasis. Moreover, patients with sporadic or familial mutations in the metavinculin-specific insert invariably develop fatal cardiomyopathies. Here we report the high resolution crystal structure of the metavinculin tail domain, as well as the crystal structures of full-length human native metavinculin (1,134 residues) and of the full-length cardiomyopathy-associated DeltaLeu954 metavinculin deletion mutant. These structures reveal that an alpha-helix (H1') and extended coil of the metavinculin insert replace alpha-helix H1 and its preceding extended coil found in the N-terminal region of the vinculin tail domain to form a new five-helix bundle tail domain. Further, biochemical analyses demonstrate that this helix replacement directs the distinct actin bundling and oligomerization properties of metavinculin. Finally, the cardiomyopathy associated DeltaLeu954 and Arg975Trp metavinculin mutants reside on the replaced extended coil and the H1' alpha-helix, respectively. Thus, a helix replacement mechanism directs metavinculin's unique functions.

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
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