1H, 13C, and 15N resonance assignment of the SPFH domain of human stomatin

Autor: Natsuko Goda, Naoko Iwaya, Yohta Kuwahara, Hidekazu Hiroaki, Yoshitaka Umetsu, Tomoyuki Tsuruta
Rok vydání: 2011
Předmět:
Zdroj: Biomolecular NMR Assignments. 6:23-25
ISSN: 1874-270X
1874-2718
Popis: 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 15N, 13C, and 1H 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.
Databáze: OpenAIRE
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