4tzl

Structure of C. elegans HTP-2 bound to HIM-3 closure motif, P21 form

spinqualitylabelsall models 4tzl, resolution 2.54Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4tzl is a 4 chain structure with sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.537Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q95XC8_CAEEL Publication Abstract from PubMed 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. The Chromosome Axis Controls Meiotic Events through a Hierarchical Assembly of HORMA Domain Proteins.,Kim Y, Rosenberg SC, Kugel CL, Kostow N, Rog O, Davydov V, Su TY, Dernburg AF, Corbett KD Dev Cell. 2014 Nov 24;31(4):487-502. doi: 10.1016/j.devcel.2014.09.013. Epub 2014, Nov 6. PMID:25446517 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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