3FQ4

Crystal structure of the Calx-beta domain of integrin beta4

3FQ4 の概要

• エントリーDOI: 10.2210/pdb3fq4/pdb
• 関連するPDBエントリー: 1QG3 3F7Q 3F7R 3FSO
• 分子名称: Integrin beta-4 (2 entities in total)
• 機能のキーワード: immunoglobulin fold, integrin, cell adhesion, alternative splicing, disease mutation, epidermolysis bullosa, glycoprotein, membrane, phosphoprotein, polymorphism, receptor, transmembrane
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: 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: 27933.33

構造登録者

Alonso-Garcia, N.,Ingles-Prieto, A.,de Pereda, J.M. (登録日: 2009-01-07, 公開日: 2009-06-23, 最終更新日: 2023-11-01)

主引用文献

Alonso-Garcia, N.,Ingles-Prieto, A.,Sonnenberg, A.,de Pereda, J.M.
Structure of the Calx-beta domain of the integrin beta4 subunit: insights into function and cation-independent stability
Acta Crystallogr.,Sect.D, 65:858-871, 2009

PubMed Abstract: The integrin alpha6beta4 is a receptor for laminins and provides stable adhesion of epithelial cells to the basement membranes. In addition, alpha6beta4 is important for keratinocyte migration during wound healing and favours the invasion of carcinomas into surrounding tissue. The cytoplasmic domain of the beta4 subunit is responsible for most of the intracellular interactions of the integrin; it contains four fibronectin type III domains and a Calx-beta motif. The crystal structure of the Calx-beta domain of beta4 was determined to 1.48 A resolution. The structure does not contain cations and biophysical data support the supposition that the Calx-beta domain of beta4 does not bind calcium. Comparison of the Calx-beta domain of beta4 with the calcium-binding domains of Na(+)/Ca(2+)-exchanger 1 reveals that in beta4 Arg1003 occupies a position equivalent to that of the calcium ions in the Na(+)/Ca(2+)-exchanger. By combining mutagenesis and thermally induced unfolding, it is shown that Arg1003 contributes to the stability of the Calx-beta domain. The structure of the Calx-beta domain is discussed in the context of the function and intracellular interactions of the integrin beta4 subunit and a putative functional site is proposed.

PubMed: 19622870
DOI: 10.1107/S0907444909018745

実験手法

X-RAY DIFFRACTION (1.487 Å)