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-Structure paper
タイトル | Molecular contacts in self-assembling clusters of membrane proteins. |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 122, Issue 26, Page e2507112122, Year 2025 |
掲載日 | 2025年6月23日 |
![]() | Venkata Shiva Mandala / Ziao Fu / Roderick MacKinnon / ![]() |
PubMed 要旨 | 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 ...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. |
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手法 | EM (単粒子) |
解像度 | 3.6 - 4.3 Å |
構造データ | EMDB-70614, PDB-9omo: EMDB-70615, PDB-9omp: ![]() EMDB-70634: human Kv2.1 reconstituted in liposomes ![]() EMDB-70635: human HCN1 reconstituted in liposomes |
由来 |
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![]() | MEMBRANE PROTEIN / GPCR / Class C / cluster |