8ZJF
Cryo-EM structure of human integrin alpha-E beta-7
Summary for 8ZJF
Entry DOI | 10.2210/pdb8zjf/pdb |
EMDB information | 60143 |
Descriptor | Integrin beta-7, Integrin alpha-E, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
Functional Keywords | complex, cryo-em, cell adhesion |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 2 |
Total formula weight | 223182.89 |
Authors | Akasaka, H.,Nureki, O.,Kise, Y. (deposition date: 2024-05-14, release date: 2024-06-05, Last modification date: 2024-10-16) |
Primary citation | Akasaka, H.,Sato, D.,Shihoya, W.,Nureki, O.,Kise, Y. Cryo-EM structure of I domain-containing integrin alpha E beta 7. Biochem.Biophys.Res.Commun., 721:150121-150121, 2024 Cited by 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 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. PubMed: 38781659DOI: 10.1016/j.bbrc.2024.150121 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.7 Å) |
Structure validation
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