Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

8B46

Crystal structure of the SUN1-KASH6 9:9 complex

Summary for 8B46
Entry DOI10.2210/pdb8b46/pdb
Related7Z8Y
DescriptorSUN domain-containing protein 1, Inositol 1,4,5-triphosphate receptor associated 2, CHLORIDE ION, ... (5 entities in total)
Functional Keywordslinc complex, nuclear structure, microtubules, structural protein
Biological sourceHomo sapiens (human)
More
Total number of polymer chains6
Total formula weight82643.45
Authors
Gurusaran, M.,Erlandsen, B.S.,Davies, O.R. (deposition date: 2022-09-19, release date: 2023-09-27, Last modification date: 2024-02-14)
Primary citationGurusaran, M.,Erlandsen, B.S.,Davies, O.R.
The crystal structure of SUN1-KASH6 reveals an asymmetric LINC complex architecture compatible with nuclear membrane insertion.
Commun Biol, 7:138-138, 2024
Cited by
PubMed Abstract: The LINC complex transmits cytoskeletal forces into the nucleus to control the structure and movement of nuclear contents. It is formed of nuclear SUN and cytoplasmic KASH proteins, which interact within the nuclear lumen, immediately below the outer nuclear membrane. However, the symmetrical location of KASH molecules within SUN-KASH complexes in previous crystal structures has been difficult to reconcile with the steric requirements for insertion of their immediately upstream transmembrane helices into the outer nuclear membrane. Here, we report the crystal structure of the SUN-KASH complex between SUN1 and JAW1/LRMP (KASH6) in an asymmetric 9:6 configuration. This intertwined assembly involves two distinct KASH conformations such that all six KASH molecules emerge on the same molecular surface. Hence, they are ideally positioned for insertion of upstream sequences into the outer nuclear membrane. Thus, we report a SUN-KASH complex architecture that appears to be directly compatible with its biological role.
PubMed: 38291267
DOI: 10.1038/s42003-024-05794-6
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.67 Å)
Structure validation

227111

數據於2024-11-06公開中

PDB statisticsPDBj update infoContact PDBjnumon