6O31

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

Summary for 6O31

Entry DOI	10.2210/pdb6o31/pdb
Descriptor	Alpha-actinin-4 (2 entities in total)
Functional Keywords	calponin homology domain, ch domain, structural protein, actin- binding protein, actin-crosslinking, glomeruloscleros spectrin family, disease mutation, nucleus, phosphorylation
Biological source	Homo sapiens (Human)
Total number of polymer chains	1
Total formula weight	26713.72
Authors	Birrane, G.,Feng, D. (deposition date: 2019-02-25, release date: 2020-02-26, Last modification date: 2023-10-11)
Primary citation	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 Cited by 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 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.51 Å)

Structure validation