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| Title | Cryo-EM structure of I domain-containing integrin αEβ7. |
|---|---|
| Journal, issue, pages | Biochem Biophys Res Commun, Vol. 721, Page 150121, Year 2024 |
| Publish date | May 14, 2024 |
 Authors | Hiroaki Akasaka / Dan Sato / Wataru Shihoya / Osamu Nureki / Yoshiaki Kise /  |
| PubMed 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 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 αEβ7, 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. |
 External links | Biochem Biophys Res Commun / PubMed:38781659 |
| Methods | EM (single particle) |
| Resolution | 2.7 Å |
| Structure data | EMDB-60143, PDB-8zjf: |
| Chemicals |  ChemComp-MG:  ChemComp-CA: |
| Source |
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 Keywords | CELL ADHESION / Complex / Cryo-EM |
homo sapiens (human)