Title :

Structure and dynamics of a human myelin protein P2 portal region mutant indicate opening of the β barrel in fatty acid binding proteins

Author(s) :

Laulumaa, Saara [Auteur]
University of Oulu
Nieminen, Tuomo [Auteur]
Tampere University of Technology [Tampere] [TUT]
Raasakka, Arne [Auteur]
University of Bergen [UiB]
Krokengen, Oda C. [Auteur]
University of Bergen [UiB]
Safaryan, Anushik [Auteur]
University of Bergen [UiB]
Hallin, Erik I. [Auteur]
University of Bergen [UiB]
Brysbaert, Guillaume [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Lensink, Marc [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Ruskamo, Salla [Auteur]
University of Oulu
Vattulainen, Ilpo [Auteur]
Tampere University of Technology [Tampere] [TUT]
Kursula, Petri [Auteur]
University of Oulu

Journal title :

BMC Structural Biology

Volume number :

18

Publication date :

2018-12

ISSN :

1472-6807

HAL domain(s) :

Chimie/Chimie théorique et/ou physique

English abstract : [en]

Myelin is a multilayered proteolipid sheath wrapped around selected axons in the nervous system. Its constituent proteins play major roles in forming of the highly regular membrane structure. P2 is a myelin-specific protein ...
Show more >Myelin is a multilayered proteolipid sheath wrapped around selected axons in the nervous system. Its constituent proteins play major roles in forming of the highly regular membrane structure. P2 is a myelin-specific protein of the fatty acid binding protein (FABP) superfamily, which is able to stack lipid bilayers together, and it is a target for mutations in the human inherited neuropathy Charcot-Marie-Tooth disease. A conserved residue that has been proposed to participate in membrane and fatty acid binding and conformational changes in FABPs is Phe57. This residue is thought to be a gatekeeper for the opening of the portal region upon ligand entry and egress.Show less >

Language :

Anglais

Audience :

Internationale

Popular science :

Non

Administrative institution(s) :

CNRS
Université de Lille

Collections :

• Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576

Research team(s) :

Computational Molecular Systems Biology

Submission date :

2020-02-12T15:45:41Z
2024-02-23T10:40:58Z