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Titre du document / Document title

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

Auteur(s) / Author(s)

Tsuruta Tomoyuki (1) ; Goda Natsuko (1 2) ; Umetsu Yoshitaka (1 2) ; Iwaya Naoko (1 3) ; Kuwahara Yohta (1 4) ; Hiroaki Hidekazu (1 2 5) ;

Affiliation(s) du ou des auteurs / Author(s) Affiliation(s)

(1) Division of Structural Biology, Graduate School of Medicine, Kobe University, Hyogo, Kobe, Japan
(2) The Structural Biology Research Center and Division of Biological Sciences, Graduate School of Science, Nagoya University, 464-8601, Nagoya, Japan
(3) Department of Molecular Engineering, Graduate School of Engineering, Kyoto University, 615-8510, Kyoto, Japan
(4) Life BEANS (Bio Electromechanical Autonomous Nano Systems) Center, BEANS Project, Tokyo, Hachioji, Japan
(5) Global-COE (Center of Excellence) Program for Integrative Membrane Biology, Kobe University, Kobe, Japan

Résumé / 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 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.

Revue / Journal Title

Biomolecular NMR assignments    ISSN  1874-270X 

Source / Source

2012, vol. 6, no1, pp. 23-25 [3 page(s) (article)]

Langue / Language

Anglais

Editeur / Publisher

Springer, Heidelberg, ALLEMAGNE  (2007) (Revue)

Mots-clés d'auteur / Author Keywords

Membrane skeleton

;

Hereditary stomatocytosis

;

SPFH domain

;

Oligomerization

;

Localisation / Location

35400061088002.0006

Springer Science+Business Media B.V., 2012
Nº notice refdoc (ud4) : 25503971



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