PDBsum entry 3h2v

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protein Protein-protein interface(s) links
Cell adhesion PDB id
Protein chains
174 a.a. *
74 a.a. *
Waters ×4
* Residue conservation analysis
PDB id:
Name: Cell adhesion
Title: Human raver1 rrm1 domain in complex with human vinculin tail domain vt
Structure: Vinculin. Chain: a, b, c, d. Fragment: c-terminal domain. Engineered: yes. Raver-1. Chain: e, f, g, h. Fragment: rrm 1 domain. Synonym: ribonucleoprotein ptb-binding 1. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: raver1, kiaa1978. Expression_system_taxid: 562
2.90Å     R-factor:   0.213     R-free:   0.277
Authors: J.H.Lee,E.S.Rangarajan,S.D.Yogesha,T.Izard
Key ref:
J.H.Lee et al. (2009). Raver1 interactions with vinculin and RNA suggest a feed-forward pathway in directing mRNA to focal adhesions. Structure, 17, 833-842. PubMed id: 19523901 DOI: 10.1016/j.str.2009.04.010
14-Apr-09     Release date:   28-Jul-09    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P18206  (VINC_HUMAN) -  Vinculin
1134 a.a.
174 a.a.*
Protein chains
Pfam   ArchSchema ?
Q8IY67  (RAVR1_HUMAN) -  Ribonucleoprotein PTB-binding 1
606 a.a.
74 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 15 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     actin cytoskeleton   1 term 
  Biological process     cell adhesion   1 term 
  Biochemical function     structural molecule activity     3 terms  


DOI no: 10.1016/j.str.2009.04.010 Structure 17:833-842 (2009)
PubMed id: 19523901  
Raver1 interactions with vinculin and RNA suggest a feed-forward pathway in directing mRNA to focal adhesions.
J.H.Lee, E.S.Rangarajan, S.D.Yogesha, T.Izard.
The translational machinery of the cell relocalizes to focal adhesions following the activation of integrin receptors. This response allows for rapid, local production of components needed for adhesion complex assembly and signaling. Vinculin links focal adhesions to the actin cytoskeleton following its activation by integrin signaling, which severs intramolecular interactions of vinculin's head and tail (Vt) domains. Our vinculin:raver1 crystal structures and binding studies show that activated Vt selectively interacts with one of the three RNA recognition motifs of raver1, that the vinculin:raver1 complex binds to F-actin, and that raver1 binds selectively to RNA, including a sequence found in vinculin mRNA. Further, mutation of residues that mediate interaction of raver1 with vinculin abolish their colocalization in cells. These findings suggest a feed-forward model where vinculin activation at focal adhesions provides a scaffold for recruitment of raver1 and its mRNA cargo to facilitate the production of components of adhesion complexes.
  Selected figure(s)  
Figure 3.
Figure 3. Structure of the Vinculin:Raver1 Complex
(A) The Vt:RRM1–3 complex structure is shown in ribbon representation, with the five α helices (H1–H5) of the tail domain of human vinculin in green, the N-terminal helix of raver1 in gray, RRM1 in blue, RRM2 in yellow, and RRM3 in red. Head-on view (left), and view rotated by 90° (right) showing the interaction of the loops connecting the β3-β2, β1-α1, and β4-β5 strands of raver1 with H2 and H3 α helices of vinculin's tail domain.
(B) The Vt:RRM1 structure showing the β-sheets and α helices of RRM1 in purple and light blue, respectively. Residues involved in the Vt-RRM1 interaction are shown on the right panel. The intermolecular hydrogen-bonding network is indicated by dotted lines. The side-chain atoms, NE and NH2, of raver1-Arg121 engage in electrostatic interactions with vinculin-Glu932 atoms OE1 and OE2, respectively, whereas raver1-Arg121 (NH1) is held in place through interactions with the main-chain oxygen of raver1-Arg119 and OD2 of vinculin-Asp953. An additional electrostatic interaction was also found between side chains of raver1-Glu120 and vinculin-Arg945, which spatially orients the side chain of vinculin-Arg945 such that it is parallel to the side chain of raver1-Arg117 and provides a stable surface for hydrophobic interaction.
Figure 6.
Figure 6. The Vinculin:Raver1 Complex Is Permissive for Binding to F-actin
Although raver1 does not bind F-actin, the Vt:raver1 complex cosediments with F-actin. After F-actin cosedimentation, supernatants (S) were removed and pellets (P, having polymerized F-actin) were washed twice.
  The above figures are reprinted by permission from Cell Press: Structure (2009, 17, 833-842) copyright 2009.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21295486 Q.Yang, M.Coseno, G.M.Gilmartin, and S.Doublié (2011).
Crystal structure of a human cleavage factor CFI(m)25/CFI(m)68/RNA complex provides an insight into poly(A) site recognition and RNA looping.
  Structure, 19, 368-377.
PDB codes: 3q2s 3q2t
20711187 C.D.Cukier, D.Hollingworth, S.R.Martin, G.Kelly, I.Díaz-Moreno, and A.Ramos (2010).
Molecular basis of FIR-mediated c-myc transcriptional control.
  Nat Struct Mol Biol, 17, 1058-1064.  
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
20112053 R.Rathinam, and S.K.Alahari (2010).
Important role of integrins in the cancer biology.
  Cancer Metastasis Rev, 29, 223-237.  
19523894 T.Madl, and M.Sattler (2009).
Adhesion dance with raver.
  Structure, 17, 781-783.  
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