8B42
Structure of heteromeric LRRC8A/C Volume-Regulated Anion Channel.
This is a non-PDB format compatible entry.
Summary for 8B42
| Entry DOI | 10.2210/pdb8b42/pdb |
| Related | 8B40 8B41 8BEN |
| EMDB information | 15835 15836 15837 15838 15839 15840 15841 |
| Descriptor | Volume-regulated anion channel subunit LRRC8A, Volume-regulated anion channel subunit LRRC8C (2 entities in total) |
| Functional Keywords | ion channel, volume-regulated anion channel, membrane protein |
| Biological source | Mus musculus (house mouse) More |
| Total number of polymer chains | 6 |
| Total formula weight | 567170.44 |
| Authors | Sawicka, M.,Dutzler, R. (deposition date: 2022-09-19, release date: 2022-12-14, Last modification date: 2025-07-02) |
| Primary citation | Rutz, S.,Deneka, D.,Dittmann, A.,Sawicka, M.,Dutzler, R. Structure of a volume-regulated heteromeric LRRC8A/C channel. Nat.Struct.Mol.Biol., 30:52-61, 2023 Cited by PubMed Abstract: Volume-regulated anion channels (VRACs) participate in the cellular response to osmotic swelling. These membrane proteins consist of heteromeric assemblies of LRRC8 subunits, whose compositions determine permeation properties. Although structures of the obligatory LRRC8A, also referred to as SWELL1, have previously defined the architecture of VRACs, the organization of heteromeric channels has remained elusive. Here we have addressed this question by the structural characterization of murine LRRC8A/C channels. Like LRRC8A, these proteins assemble as hexamers. Despite 12 possible arrangements, we find a predominant organization with an A:C ratio of two. In this assembly, four LRRC8A subunits cluster in their preferred conformation observed in homomers, as pairs of closely interacting proteins that stabilize a closed state of the channel. In contrast, the two interacting LRRC8C subunits show a larger flexibility, underlining their role in the destabilization of the tightly packed A subunits, thereby enhancing the activation properties of the protein. PubMed: 36522427DOI: 10.1038/s41594-022-00899-0 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (6.6 Å) |
Structure validation
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