4WTW

Crystal structure of the third FnIII domain of integrin beta4

4WTW の概要

• エントリーDOI: 10.2210/pdb4wtw/pdb
• 関連するPDBエントリー: 2YRZ
• 分子名称: Integrin beta-4, SULFATE ION, PENTAETHYLENE GLYCOL, ... (5 entities in total)
• 機能のキーワード: immunoglobulin fold, fibronectin type iii, integrin, cell adhesion
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cell membrane; Single-pass type I membrane protein: P16144
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22166.80

構造登録者

Alonso-Garcia, N.,Urien, H.,de Pereda, J.M. (登録日: 2014-10-30, 公開日: 2015-02-11, 最終更新日: 2024-01-10)

主引用文献

Alonso-Garcia, N.,Garcia-Rubio, I.,Manso, J.A.,Buey, R.M.,Urien, H.,Sonnenberg, A.,Jeschke, G.,de Pereda, J.M.
Combination of X-ray crystallography, SAXS and DEER to obtain the structure of the FnIII-3,4 domains of integrin alpha6beta4
Acta Crystallogr.,Sect.D, 71:969-985, 2015

PubMed 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.

PubMed: 25849406
DOI: 10.1107/S1399004715002485

実験手法

X-RAY DIFFRACTION (1.606 Å)