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4TZS

Structure of C. elegans HTP-2 bound to HIM-3 closure motif, P212121 form

Summary for 4TZS
Entry DOI10.2210/pdb4tzs/pdb
Related4TRK 4TZJ 4TZL 4TZM 4TZN 4TZO 4TZQ
DescriptorProtein HTP-2, C. elegans HIM-3 closure motif (3 entities in total)
Functional Keywordshorma domain, meiosis, chromosome axis, peptide binding protein
Biological sourceCaenorhabditis elegans
More
Total number of polymer chains4
Total formula weight61855.37
Authors
Rosenberg, S.C.,Corbett, K.D. (deposition date: 2014-07-10, 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 (2.55 Å)
Structure validation

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