6OA6

CRYSTAL STRUCTURE OF THE ACTIN-BINDING DOMAIN OF HUMAN ALPHA-ACTININ-4

6OA6 の概要

• エントリーDOI: 10.2210/pdb6oa6/pdb
• 関連するPDBエントリー: 2R0O 6O31
• 分子名称: Alpha-actinin-4, GLYCEROL (3 entities in total)
• 機能のキーワード: calponin homology domain, ch domain, structural protein, actin- binding protein, actin-crosslinking, glomeruloscleros spectrin family, disease mutation, nucleus, phosphorylation
• 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: 26833.82

構造登録者

Birrane, G.,Feng, D. (登録日: 2019-03-15, 公開日: 2020-03-18, 最終更新日: 2023-10-11)

主引用文献

Feng, D.,Kumar, M.,Muntel, J.,Gurley, S.B.,Birrane, G.,Stillman, I.E.,Ding, L.,Wang, M.,Ahmed, S.,Schlondorff, J.,Alper, S.L.,Ferrante, T.,Marquez, S.L.,Ng, C.F.,Novak, R.,Ingber, D.E.,Steen, H.,Pollak, M.R.
Phosphorylation of ACTN4 Leads to Podocyte Vulnerability and Proteinuric Glomerulosclerosis.
J. Am. Soc. Nephrol., 31:1479-1495, 2020

PubMed Abstract: Genetic mutations in -actinin-4 (ACTN4)-an important actin crosslinking cytoskeletal protein that provides structural support for kidney podocytes-have been linked to proteinuric glomerulosclerosis in humans. However, the effect of post-translational modifications of ACTN4 on podocyte integrity and kidney function is not known.

PubMed: 32540856
DOI: 10.1681/ASN.2019101032

実験手法

X-RAY DIFFRACTION (1.37 Å)