6R15
Crystal structure of the SUN1-KASH1 6:6 complex
Summary for 6R15
Entry DOI | 10.2210/pdb6r15/pdb |
Descriptor | SUN domain-containing protein 1, Nesprin-1, POTASSIUM ION, ... (6 entities in total) |
Functional Keywords | sun1 kash1 nesprin-1 syne1 linc complex nucleoskeleton cytoskeleton nuclear envelope, structural protein |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 2 |
Total formula weight | 26563.96 |
Authors | Gurusaran, M.,Davies, O.R. (deposition date: 2019-03-13, release date: 2020-04-01, Last modification date: 2024-11-13) |
Primary citation | Gurusaran, M.,Davies, O.R. A molecular mechanism for LINC complex branching by structurally diverse SUN-KASH 6:6 assemblies. Elife, 10:-, 2021 Cited by PubMed Abstract: The Linker of Nucleoskeleton and Cytoskeleton (LINC) complex mechanically couples cytoskeletal and nuclear components across the nuclear envelope to fulfil a myriad of cellular functions, including nuclear shape and positioning, hearing, and meiotic chromosome movements. The canonical model is that 3:3 interactions between SUN and KASH proteins underlie the nucleocytoskeletal linkages provided by the LINC complex. Here, we provide crystallographic and biophysical evidence that SUN-KASH is a constitutive 6:6 complex in which two constituent 3:3 complexes interact head-to-head. A common SUN-KASH topology is achieved through structurally diverse 6:6 interaction mechanisms by distinct KASH proteins, including zinc-coordination by Nesprin-4. The SUN-KASH 6:6 interface provides a molecular mechanism for the establishment of integrative and distributive connections between 3:3 structures within a branched LINC complex network. In this model, SUN-KASH 6:6 complexes act as nodes for force distribution and integration between adjacent SUN and KASH molecules, enabling the coordinated transduction of large forces across the nuclear envelope. PubMed: 33393904DOI: 10.7554/eLife.60175 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.82 Å) |
Structure validation
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