title: ¹H, ¹³C, and ¹⁵N resonance assignment of the SPFH domain of human stomatin.
abstract: Stomatin, a 288-residue protein, is a component of the membrane skeleton of red blood cells (RBCs), which helps to physically support the membrane and maintains its function. In RBCs, stomatin binds to the glucose transporter GLUT-1 and may regulate its function. Stomatin has a stomatin/prohibitin/flotillin/HflK (SPFH) domain at the center of its polypeptide chain. There are 12 SPFH domain-containing proteins, most of which are localized at the cellular or subcellular membranes. Although the molecular function of the SPFH domain has not yet been established, the domain may be involved in protein oligomerization. The SPFH domain of the archaeal stomatin homolog has been shown to form unique oligomers. Here we report the (15)N, (13)C, and (1)H chemical shift assignments of the SPFH domain of human stomatin [hSTOM(SPFH)]. These may help in determining the structure of hSTOM(SPFH) in solution as well as in clarifying its involvement in protein oligomerization.
authors.affiliation: Division of Structural Biology, Graduate School of Medicine, Kobe University, 7-5-1, Kusunoki-cho, Chuo-ku, Kobe, Hyogo 650-0017, Japan.
authors.forename: Tomoyuki
authors.initials: T
authors.lastname: Tsuruta
authors.forename: Natsuko
authors.initials: N
authors.lastname: Goda
authors.forename: Yoshitaka
authors.initials: Y
authors.lastname: Umetsu
authors.forename: Naoko
authors.initials: N
authors.lastname: Iwaya
authors.forename: Yohta
authors.initials: Y
authors.lastname: Kuwahara
authors.forename: Hidekazu
authors.initials: H
authors.lastname: Hiroaki
mesh_terms: D004912:Erythrocytes / Q000378:metabolism; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary
chemical_list: D008565:Membrane Proteins; C036860:STOM protein, human