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PDBsum entry 3myi

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protein links
Cell adhesion PDB id
3myi
Jmol
Contents
Protein chain
163 a.a. *
Waters ×93
* Residue conservation analysis
PDB id:
3myi
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
Resolution:
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
Date:
10-May-10     Release date:   26-May-10    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P18206  (VINC_HUMAN) -  Vinculin
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
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.
 
  ABSTRACT  
 
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
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.