Cargando…
Structural and mutational studies suggest key residues to determine whether stomatin SPFH domains form dimers or trimers
Stomatin is a major integral membrane protein in human erythrocytes. In a form of hemolytic anemia known as hereditary stomatocytosis, stomatin is deficient in the erythrocyte membrane due to mis-trafficking. It is a member of stomatin, prohibitin, flotillin, and HflK/C (SPFH) domain proteins, and S...
Autores principales: | Komatsu, Tomoya, Matsui, Ikuo, Yokoyama, Hideshi |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9663324/ https://www.ncbi.nlm.nih.gov/pubmed/36386441 http://dx.doi.org/10.1016/j.bbrep.2022.101384 |
Ejemplares similares
-
Novel dimer structure of a membrane-bound protease with a catalytic Ser–Lys dyad and its linkage to stomatin
por: Yokoyama, Hideshi, et al.
Publicado: (2008) -
Crystal structure of the stomatin operon partner protein from Pyrococcus horikoshii indicates the formation of a multimeric assembly
por: Yokoyama, Hideshi, et al.
Publicado: (2014) -
A cryptic phosphate-binding pocket on the SPFH domain of human stomatin that regulates a novel fibril-like self-assembly
por: Kataoka, Koki, et al.
Publicado: (2022) -
Structural and biochemical analysis of a thermostable membrane-bound stomatin-specific protease
por: Yokoyama, Hideshi, et al.
Publicado: (2013) -
Higher‐order structure formation using refined monomer structures of lipid raft markers, Stomatin, Prohibitin, Flotillin, and HflK/C‐related proteins
por: Yokoyama, Hideshi, et al.
Publicado: (2023)