1V05

Dimerization of human Filamin C: crystal structure of the domain 24

1V05 の概要

• エントリーDOI: 10.2210/pdb1v05/pdb
• 分子名称: FILAMIN C (2 entities in total)
• 機能のキーワード: actin-binding protein, immunoglobulin
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10382.99

構造登録者

Pudas, R.,Kiema, T.-R.,Ylanne, J. (登録日: 2004-03-22, 公開日: 2004-11-17, 最終更新日: 2024-05-08)

主引用文献

Pudas, R.,Kiema, T.-R.,Butler, P.J.G.,Stewart, M.,Ylanne, J.
Structural Basis for Vertebrate Filamin Dimerization
Structure, 13:111-, 2005

PubMed Abstract: Filamins are essential in cell motility and many developmental processes. They are large actin cross linking proteins that contain actin binding domains in their N termini and a long rod region constructed from 24 tandem Ig domains. Dimerization is crucial for the actin crosslinking function of filamins and requires the most C-terminal Ig domain. We describe here the crystal structure of this 24th Ig domain (Ig24) of human filamin C and show how it mediates dimerization. The dimer interface is novel and quite different to that seen in the Dictyostelium discoideum filamin analog. The sequence signature of the dimerization interface suggests that the C-terminal domains of all vertebrate filamins share the same dimerization mechanism. Furthermore, we show that point mutations in the dimerization interface disrupt the dimer and that the dissociation constant for recombinant Ig24 is in the micromolar range.

PubMed: 15642266
DOI: 10.1016/J.STR.2004.10.014

実験手法

X-RAY DIFFRACTION (1.43 Å)