PDBsum entry 4wtx

Cell adhesion

PDB id: 4wtx

Contents

Protein chain

97 a.a.

Waters ×122

PDB id:

4wtx

Name:

Cell adhesion

Title:

Crystal structure of the fourth fniii domain of integrin beta4

Structure:

Integrin beta-4. Chain: a. Fragment: fourth fniii domain, unp residues 1572-1666. Synonym: gp150. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: itgb4. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

1.50Å R-factor: 0.196 R-free: 0.218

Authors:

N.Alonso-Garcia,H.Urien,R.M.Buey,J.M.De Pereda

Key ref:

N.Alonso-García et al. (2015). Combination of X-ray crystallography, SAXS and DEER to obtain the structure of the FnIII-3,4 domains of integrin α6β4. Acta Crystallogr D Biol Crystallogr, 71, 969-985. PubMed id: 25849406 DOI: 10.1107/S1399004715002485

Date:

30-Oct-14 Release date: 11-Feb-15

Protein chain

P16144  (ITB4_HUMAN) -  Integrin beta-4 from Homo sapiens

Seq: 1822 a.a.

Struc: 97 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

DOI no: 10.1107/S1399004715002485

Acta Crystallogr D Biol Crystallogr 71:969-985 (2015)

PubMed id: 25849406

Combination of X-ray crystallography, SAXS and DEER to obtain the structure of the FnIII-3,4 domains of integrin α6β4.

N.Alonso-García, I.García-Rubio, J.A.Manso, R.M.Buey, H.Urien, A.Sonnenberg, G.Jeschke, J.M.de Pereda.

ABSTRACT

Integrin α6β4 is a major component of hemidesmosomes that mediate the stable anchorage of epithelial cells to the underlying basement membrane. Integrin α6β4 has also been implicated in cell proliferation and migration and in carcinoma progression. The third and fourth fibronectin type III domains (FnIII-3,4) of integrin β4 mediate binding to the hemidesmosomal proteins BPAG1e and BPAG2, and participate in signalling. Here, it is demonstrated that X-ray crystallography, small-angle X-ray scattering and double electron-electron resonance (DEER) complement each other to solve the structure of the FnIII-3,4 region. The crystal structures of the individual FnIII-3 and FnIII-4 domains were solved and the relative arrangement of the FnIII domains was elucidated by combining DEER with site-directed spin labelling. Multiple structures of the interdomain linker were modelled by Monte Carlo methods complying with DEER constraints, and the final structures were selected against experimental scattering data. FnIII-3,4 has a compact and cambered flat structure with an evolutionary conserved surface that is likely to correspond to a protein-interaction site. Finally, this hybrid method is of general application for the study of other macromolecules and complexes.