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PDBsum entry 5ayq

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protein Protein-protein interface(s) links
Metal transport PDB id
5ayq

 

 

 

 

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Contents
Protein chains
118 a.a.
Waters ×230
PDB id:
5ayq
Name: Metal transport
Title: Structure-based site-directed photo-crosslinking analyses of multimeric cell-adhesive interactions of vgsc beta subunits
Structure: Sodium channel subunit beta-4. Chain: a, b. Fragment: unp residues 30-160. Engineered: yes
Source: Mus musculus. Mouse. Organism_taxid: 10090. Gene: scn4b, gm1471. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.70Å     R-factor:   0.205     R-free:   0.231
Authors: H.Shimizu
Key ref: H.Shimizu et al. (2016). Structure-based site-directed photo-crosslinking analyses of multimeric cell-adhesive interactions of voltage-gated sodium channel β subunits. Sci Rep, 6, 26618. PubMed id: 27216889 DOI: 10.1038/srep26618
Date:
01-Sep-15     Release date:   08-Jun-16    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q7M729  (SCN4B_MOUSE) -  Sodium channel subunit beta-4 from Mus musculus
Seq:
Struc:
228 a.a.
118 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1038/srep26618 Sci Rep 6:26618 (2016)
PubMed id: 27216889  
 
 
Structure-based site-directed photo-crosslinking analyses of multimeric cell-adhesive interactions of voltage-gated sodium channel β subunits.
H.Shimizu, H.Miyazaki, N.Ohsawa, S.Shoji, Y.Ishizuka-Katsura, A.Tosaki, F.Oyama, T.Terada, K.Sakamoto, M.Shirouzu, S.Sekine, N.Nukina, S.Yokoyama.
 
  ABSTRACT  
 
The β1, β2, and β4 subunits of voltage-gated sodium channels reportedly function as cell adhesion molecules. The present crystallographic analysis of the β4 extracellular domain revealed an antiparallel arrangement of the β4 molecules in the crystal lattice. The interface between the two antiparallel β4 molecules is asymmetric, and results in a multimeric assembly. Structure-based mutagenesis and site-directed photo-crosslinking analyses of the β4-mediated cell-cell adhesion revealed that the interface between the antiparallel β4 molecules corresponds to that in the trans homophilic interaction for the multimeric assembly of β4 in cell-cell adhesion. This trans interaction mode is also employed in the β1-mediated cell-cell adhesion. Moreover, the β1 gene mutations associated with generalized epilepsy with febrile seizures plus (GEFS+) impaired the β1-mediated cell-cell adhesion, which should underlie the GEFS+ pathogenesis. Thus, the structural basis for the β-subunit-mediated cell-cell adhesion has been established.
 

 

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