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Nature

Resumen/Descripción – provisto por la editorial en inglés

Nature is a weekly international journal publishing the finest peer-reviewed research in all fields of science and technology on the basis of its originality, importance, interdisciplinary interest, timeliness, accessibility, elegance and surprising conclusions. Nature also provides rapid, authoritative, insightful and arresting news and interpretation of topical and coming trends affecting science, scientists and the wider public.

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No detectada	desde jul. 2012 / hasta dic. 2023	Nature.com
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Información

Tipo de recurso:

revistas

ISSN impreso

0028-0836

ISSN electrónico

1476-4687

Editor responsable

Springer Nature

País de edición

Reino Unido

Fecha de publicación

1869-

Cobertura temática

Ciencias naturales

Ingeniería y tecnología

Ciencias médicas y de la salud

Ciencias agrícolas y veterinarias

Tabla de contenidos

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doi: 10.1038/s41586-021-03641-w

Structures of human mGlu2 and mGlu7 homo- and heterodimers

Juan Du; Dejian Wang; Hongcheng Fan; Chanjuan Xu; Linhua Tai; Shuling Lin; Shuo Han; Qiuxiang Tan; Xinwei Wang; Tuo Xu; Hui Zhang; Xiaojing Chu; Cuiying Yi; Peng Liu; Xiaomei Wang; Yu Zhou; Jean-Philippe Pin; Philippe Rondard; Hong Liu; Jianfeng Liu; Fei Sun; Beili Wu; Qiang Zhao

Palabras clave: Multidisciplinary.

Pp. 589-593

doi: 10.1038/s41586-021-03507-1

Structural basis of GABAB receptorâ€“Gi protein coupling

Cangsong Shen; Chunyou Mao; Chanjuan Xu; Nan Jin; Huibing Zhang; Dan-Dan Shen; Qingya Shen; Xiaomei Wang; Tingjun Hou; Zhong Chen; Philippe Rondard; Jean-Philippe Pin; Yan Zhang; Jianfeng Liu

<jats:title>Abstract</jats:title><jats:p>G-protein-coupled receptors (GPCRs) have central roles in intercellular communication<jats:sup>1,2</jats:sup>. Structural studies have revealed how GPCRs can activate GÂ proteins. However, whether this mechanism is conserved among all classes of GPCR remains unknown. Here we report the structure of the class-C heterodimeric GABA<jats:sub>B</jats:sub> receptor, which is activated by the inhibitory transmitter GABA, in its active form complexed with G<jats:sub>i1</jats:sub> protein. We found that a single GÂ protein interacts with the GB2 subunit of the GABA<jats:sub>B</jats:sub> receptor at a site that mainly involves intracellular loopÂ 2 on the side of the transmembrane domain. This is in contrast to the GÂ protein binding in a central cavity, as has been observed with other classes of GPCR. This binding mode results from the active form of the transmembrane domain of this GABA<jats:sub>B</jats:sub> receptor being different from that of other GPCRs, as it shows no outside movement of transmembrane helixÂ 6. Our work also provides details of the inter- and intra-subunit changes that link agonist binding to G-protein activation in this heterodimeric complex.</jats:p>

Palabras clave: Multidisciplinary.

Pp. 594-598