6j07

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Current revision (15:26, 27 February 2019) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 6j07 is ON HOLD until Paper Publication
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==Crystal structure of human TERB2 and TERB1==
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<StructureSection load='6j07' size='340' side='right' caption='[[6j07]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6j07]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J07 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6J07 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5xup|5xup]]</td></tr>
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<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=6j07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j07 OCA], [http://pdbe.org/6j07 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6j07 RCSB], [http://www.ebi.ac.uk/pdbsum/6j07 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6j07 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/TERB2_HUMAN TERB2_HUMAN]] Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis. Component of the MAJIN-TERB1-TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA.[UniProtKB:Q9D494] [[http://www.uniprot.org/uniprot/TERB1_HUMAN TERB1_HUMAN]] Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis. Component of the MAJIN-TERB1-TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA. In the MAJIN-TERB1-TERB2 complex, TERB1 probably mediates association with the shelterin/telosome complex via interaction with TERF1, promoting priming telomeric DNA attachment'. Promotes telomere association with the nuclear envelope and deposition of the SUN-KASH/LINC complex. Also recruits cohesin to telomeres to develop structural rigidity.[UniProtKB:Q8C0V1]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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During meiotic prophase I, telomeres attach to and move on the nuclear envelope (NE), regulating chromosome movement to promote homologous pairing. Meiosis-specific proteins TERB1, TERB2 and MAJIN play a key role in this process. Here, we report the crystal structures of human TERB1-TERB2 and TERB2-MAJIN subcomplexes. Specific disruption of the TERB1-TERB2 or the TERB2-MAJIN interaction in the mouse Terb2 gene abolishes the telomere attachment to the NE and causes aberrant homologous pairing and disordered synapsis. In addition, depletion of SUN1 also partially disrupts the telomere-NE connection. We propose that the telomere-TRF1-TERB1-TERB2-MAJIN-NE interaction network and the telomere-LINC complex connection are likely two separate but cooperative pathways to stably recruit telomeres to the NE in meiosis prophase I. Our work provides a molecular model of the connection between telomeres and the NE and reveals the correlation between aberrant synapsis and the defective telomere attachment to the NE.
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Authors: Wang, Y., Chen, Y., Wu, J., Huang, C., Lei, M.
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The meiotic TERB1-TERB2-MAJIN complex tethers telomeres to the nuclear envelope.,Wang Y, Chen Y, Chen J, Wang L, Nie L, Long J, Chang H, Wu J, Huang C, Lei M Nat Commun. 2019 Feb 4;10(1):564. doi: 10.1038/s41467-019-08437-1. PMID:30718482<ref>PMID:30718482</ref>
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Description: Crystal structure of human TERB2 and TERB1
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Wang, Y]]
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<div class="pdbe-citations 6j07" style="background-color:#fffaf0;"></div>
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[[Category: Lei, M]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Chen, Y]]
[[Category: Chen, Y]]
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[[Category: Wu, J]]
 
[[Category: Huang, C]]
[[Category: Huang, C]]
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[[Category: Lei, M]]
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[[Category: Wang, Y]]
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[[Category: Wu, J]]
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[[Category: Dna binding protein]]
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[[Category: Meiosis]]
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[[Category: Nuclear envelope attachment]]
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[[Category: Protein-protein complex]]
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[[Category: Telomere]]

Current revision

Crystal structure of human TERB2 and TERB1

6j07, resolution 3.30Å

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