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| | <StructureSection load='4tzq' size='340' side='right'caption='[[4tzq]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='4tzq' size='340' side='right'caption='[[4tzq]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4tzq]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TZQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TZQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4tzq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TZQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TZQ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4trk|4trk]], [[4tzj|4tzj]], [[4tzl|4tzl]], [[4tzm|4tzm]], [[4tzn|4tzn]], [[4tzo|4tzo]], [[4tzs|4tzs]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">htp-1, CELE_F41H10.10, F41H10.10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL]), htp-3, CELE_F57C9.5, F57C9.5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4tzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tzq OCA], [https://pdbe.org/4tzq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tzq RCSB], [https://www.ebi.ac.uk/pdbsum/4tzq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tzq ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tzq OCA], [http://pdbe.org/4tzq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tzq RCSB], [http://www.ebi.ac.uk/pdbsum/4tzq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tzq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O01820_CAEEL O01820_CAEEL] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Caeel]] | + | [[Category: Caenorhabditis elegans]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Corbett, K D]] | + | [[Category: Corbett KD]] |
| - | [[Category: Rosenberg, S C]] | + | [[Category: Rosenberg SC]] |
| - | [[Category: Chromosome axis]]
| + | |
| - | [[Category: Horma domain]]
| + | |
| - | [[Category: Meiosis]]
| + | |
| - | [[Category: Peptide binding protein]]
| + | |
| Structural highlights
Function
O01820_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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kim Y, Rosenberg SC, Kugel CL, Kostow N, Rog O, Davydov V, Su TY, Dernburg AF, Corbett KD. The Chromosome Axis Controls Meiotic Events through a Hierarchical Assembly of HORMA Domain Proteins. Dev Cell. 2014 Nov 24;31(4):487-502. doi: 10.1016/j.devcel.2014.09.013. Epub 2014, Nov 6. PMID:25446517 doi:http://dx.doi.org/10.1016/j.devcel.2014.09.013
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