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Cryo-EM structure of I domain-containing integrin αEß7.
Akasaka, Hiroaki; Sato, Dan; Shihoya, Wataru; Nureki, Osamu; Kise, Yoshiaki.
Afiliación
  • Akasaka H; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Bunkyo, Tokyo, 113-0033, Japan.
  • Sato D; Curreio, Inc., Room 357, South Clinical Research Laboratory, The University of Tokyo, 7-3-1, Hongo, Bunkyo-ku, Tokyo, 113-8485, Japan.
  • Shihoya W; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Bunkyo, Tokyo, 113-0033, Japan.
  • Nureki O; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Bunkyo, Tokyo, 113-0033, Japan; Curreio, Inc., Room 357, South Clinical Research Laboratory, The University of Tokyo, 7-3-1, Hongo, Bunkyo-ku, Tokyo, 113-8485, Japan. Electronic address: nureki@bs.s.u-tokyo.ac.jp
  • Kise Y; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Bunkyo, Tokyo, 113-0033, Japan; Curreio, Inc., Room 357, South Clinical Research Laboratory, The University of Tokyo, 7-3-1, Hongo, Bunkyo-ku, Tokyo, 113-8485, Japan. Electronic address: yoshiaki.kise@curreio.com
Biochem Biophys Res Commun ; 721: 150121, 2024 08 20.
Article en En | MEDLINE | ID: mdl-38781659
ABSTRACT
The integrin family is a transmembrane receptor that plays critical roles in the cell-cell and cell-extracellular matrix adhesion, signal transduction such as cell cycle regulation, organization of the intracellular cytoskeleton, and immune responses. Consequently, dysfunction of integrins is associated with a wide range of human diseases, including cancer and immune diseases, which makes integrins therapeutic targets for drug discovery. Here we report the cryo-EM structure of the human α-I domain-containing full-length integrin αEß7, which is expressed in the leukocytes of the immune system and a drug target for inflammatory bowel disease (IBD). The structure reveals the half-bent conformation, an intermediate between the close and the open conformation, while the α-I domain responsible for the ligand binding covers the headpiece domain by a unique spatial arrangement. Our results provide the structural information for the drug design targeting IBD.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Modelos Moleculares / Microscopía por Crioelectrón / Dominios Proteicos Límite: Humans Idioma: En Revista: Biochem Biophys Res Commun Año: 2024 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Modelos Moleculares / Microscopía por Crioelectrón / Dominios Proteicos Límite: Humans Idioma: En Revista: Biochem Biophys Res Commun Año: 2024 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos