8AU0
Crystal structure of the a1 luminal coiled-coil domain of SUN1
Summary for 8AU0
| Entry DOI | 10.2210/pdb8au0/pdb |
| Descriptor | SUN domain-containing protein 1 (2 entities in total) |
| Functional Keywords | linc complex, nuclear structure, microtubules, structural protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 3 |
| Total formula weight | 13959.59 |
| Authors | Gurusaran, M.,Davies, O.R. (deposition date: 2022-08-24, release date: 2023-07-19, Last modification date: 2024-11-06) |
| Primary citation | Gurusaran, M.,Biemans, J.J.,Wood, C.W.,Davies, O.R. Molecular insights into LINC complex architecture through the crystal structure of a luminal trimeric coiled-coil domain of SUN1. Front Cell Dev Biol, 11:1144277-1144277, 2023 Cited by PubMed Abstract: The LINC complex, consisting of interacting SUN and KASH proteins, mechanically couples nuclear contents to the cytoskeleton. In meiosis, the LINC complex transmits microtubule-generated forces to chromosome ends, driving the rapid chromosome movements that are necessary for synapsis and crossing over. In somatic cells, it defines nuclear shape and positioning, and has a number of specialised roles, including hearing. Here, we report the X-ray crystal structure of a coiled-coiled domain of SUN1's luminal region, providing an architectural foundation for how SUN1 traverses the nuclear lumen, from the inner nuclear membrane to its interaction with KASH proteins at the outer nuclear membrane. In combination with light and X-ray scattering, molecular dynamics and structure-directed modelling, we present a model of SUN1's entire luminal region. This model highlights inherent flexibility between structured domains, and raises the possibility that domain-swap interactions may establish a LINC complex network for the coordinated transmission of cytoskeletal forces. PubMed: 37416798DOI: 10.3389/fcell.2023.1144277 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.07 Å) |
Structure validation
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