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4TRK

Structure of C. elegans HIM-3

Summary for 4TRK
Entry DOI10.2210/pdb4trk/pdb
DescriptorC. elegans HIM-3 (2 entities in total)
Functional Keywordshorma domain, meiosis, chromosome axis, dna binding protein
Biological sourceCaenorhabditis elegans
Total number of polymer chains1
Total formula weight33166.83
Authors
Rosenberg, S.C.,Corbett, K.D. (deposition date: 2014-06-17, release date: 2014-11-19, Last modification date: 2023-12-27)
Primary citationKim, Y.,Rosenberg, S.C.,Kugel, C.L.,Kostow, N.,Rog, O.,Davydov, V.,Su, T.Y.,Dernburg, A.F.,Corbett, K.D.
The Chromosome Axis Controls Meiotic Events through a Hierarchical Assembly of HORMA Domain Proteins.
Dev.Cell, 31:487-502, 2014
Cited by
PubMed Abstract: Proteins of the HORMA domain family play central, but poorly understood, roles in chromosome organization and dynamics during meiosis. In Caenorhabditis elegans, four such proteins (HIM-3, HTP-1, HTP-2, and HTP-3) have distinct but overlapping functions. Through combined biochemical, structural, and in vivo analysis, we find that these proteins form hierarchical complexes through binding of their HORMA domains to cognate peptides within their partners' C-terminal tails, analogous to the "safety belt" binding mechanism of Mad2. These interactions are critical for recruitment of HIM-3, HTP-1, and HTP-2 to chromosome axes. HTP-3, in addition to recruiting the other HORMA domain proteins to the axis, plays an independent role in sister chromatid cohesion and double-strand break formation. Finally, we find that mammalian HORMAD1 binds a motif found both at its own C terminus and at that of HORMAD2, indicating that this mode of intermolecular association is a conserved feature of meiotic chromosome structure in eukaryotes.
PubMed: 25446517
DOI: 10.1016/j.devcel.2014.09.013
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.751 Å)
Structure validation

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