9OMP
mGluR7 in native membrane vesicles
Summary for 9OMP
| Entry DOI | 10.2210/pdb9omp/pdb |
| EMDB information | 70615 |
| Descriptor | Metabotropic glutamate receptor 7 (1 entity in total) |
| Functional Keywords | gpcr, class c, membrane protein, cluster |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 205669.88 |
| Authors | |
| Primary citation | Mandala, V.S.,Fu, Z.,MacKinnon, R. Molecular contacts in self-assembling clusters of membrane proteins. Proc.Natl.Acad.Sci.USA, 122:e2507112122-e2507112122, 2025 Cited by PubMed Abstract: Motivated by recent data pointing to the existence of homo-oligomeric assemblies of membrane proteins called higher-order transient structures, and their apparent role in connecting components of membrane signal pathways, we examine here by cryoelectron microscopy some of the protein-protein interactions that occur in cluster formation. Metabotropic glutamate receptors and HCN ion channels inside clusters contact their neighbors through structured extracellular and intracellular domains, respectively. Other ion channels, including Kv2.1 and Slo1, appear to form clusters through prominent intrinsically disordered sequences in the cytoplasm. These distinct modes of interaction are associated with clusters exhibiting varying degrees of compactness and order. We conclude that nature utilizes a variety of ways to form connections between membrane proteins in self-assembled clusters. PubMed: 40549920DOI: 10.1073/pnas.2507112122 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.3 Å) |
Structure validation
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