Your browser doesn't support javascript.
loading
Structural insights into the ligand binding domain of GluD1 and GluD2 receptors.
Tricoire, Ludovic; Hepp, Régine.
Afiliación
  • Tricoire L; INSERM, CNRS, Neuroscience Paris Seine - Institut de Biologie Paris Seine, Sorbonne Université, Paris, France.
  • Hepp R; INSERM, CNRS, Neuroscience Paris Seine - Institut de Biologie Paris Seine, Sorbonne Université, Paris, France.
FEBS J ; 290(15): 3745-3747, 2023 08.
Article en En | MEDLINE | ID: mdl-37345272
ABSTRACT
GluD1 and GluD2 subunits (also known as delta 1 and 2) are the members of the delta family of ionotropic glutamate receptors. They are particularly puzzling, since they are unable to bind glutamate, but rather bind glycine and d-serine via their classical ligand binding domain (LBD). While GluD2 has been the subject of intensive research over the past decades, it is only recently that GluD1 received similar interest and very few studies compare the properties of these two membrane proteins. In their research article included in this issue, Masternak et al. resolved the 3D structure of the GluD1 LBD, compared its d-serine sensitivity with that of GluD2 and identified critical residues involved in the dynamics of the LBD.
Asunto(s)
Palabras clave

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Receptores de Glutamato / Ácido Glutámico Idioma: En Revista: FEBS J Asunto de la revista: BIOQUIMICA Año: 2023 Tipo del documento: Article País de afiliación: Francia

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Receptores de Glutamato / Ácido Glutámico Idioma: En Revista: FEBS J Asunto de la revista: BIOQUIMICA Año: 2023 Tipo del documento: Article País de afiliación: Francia
...