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| | ==Crystal structure of the chicken Spc24-Spc25 globular domain== | | ==Crystal structure of the chicken Spc24-Spc25 globular domain== |
| - | <StructureSection load='3vz9' size='340' side='right' caption='[[3vz9]], [[Resolution|resolution]] 1.03Å' scene=''> | + | <StructureSection load='3vz9' size='340' side='right'caption='[[3vz9]], [[Resolution|resolution]] 1.03Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3vz9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VZ9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VZ9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3vz9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VZ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VZ9 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vza|3vza]]</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]] 1.03Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SPC25 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK])</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=3vz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vz9 OCA], [https://pdbe.org/3vz9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vz9 RCSB], [https://www.ebi.ac.uk/pdbsum/3vz9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vz9 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=3vz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vz9 OCA], [http://pdbe.org/3vz9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vz9 RCSB], [http://www.ebi.ac.uk/pdbsum/3vz9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vz9 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/E1C4Y2_CHICK E1C4Y2_CHICK] |
| | <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: Chick]] | + | [[Category: Gallus gallus]] |
| - | [[Category: Fukagawa, T]] | + | [[Category: Large Structures]] |
| - | [[Category: Nishino, T]] | + | [[Category: Fukagawa T]] |
| - | [[Category: Cell cycle]] | + | [[Category: Nishino T]] |
| - | [[Category: Chromosome segregation]]
| + | |
| - | [[Category: Kinetochore component]]
| + | |
| - | [[Category: Ndc80 complex]]
| + | |
| - | [[Category: Rwd domain]]
| + | |
| Structural highlights
Function
E1C4Y2_CHICK
Publication Abstract from PubMed
The kinetochore forms a dynamic interface with microtubules from the mitotic spindle during mitosis. The Ndc80 complex acts as the key microtubule-binding complex at kinetochores. However, it is unclear how the Ndc80 complex associates with the inner kinetochore proteins that assemble upon centromeric chromatin. Here, based on a high-resolution structural analysis, we demonstrate that the N-terminal region of vertebrate CENP-T interacts with the 'RWD' domain in the Spc24/25 portion of the Ndc80 complex. Phosphorylation of CENP-T strengthens a cryptic hydrophobic interaction between CENP-T and Spc25 resulting in a phospho-regulated interaction that occurs without direct recognition of the phosphorylated residue. The Ndc80 complex interacts with both CENP-T and the Mis12 complex, but we find that these interactions are mutually exclusive, supporting a model in which two distinct pathways target the Ndc80 complex to kinetochores. Our results provide a model for how the multiple protein complexes at kinetochores associate in a phospho-regulated manner.
CENP-T provides a structural platform for outer kinetochore assembly.,Nishino T, Rago F, Hori T, Tomii K, Cheeseman IM, Fukagawa T EMBO J. 2013 Feb 6;32(3):424-36. doi: 10.1038/emboj.2012.348. Epub 2013 Jan 18. PMID:23334297[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nishino T, Rago F, Hori T, Tomii K, Cheeseman IM, Fukagawa T. CENP-T provides a structural platform for outer kinetochore assembly. EMBO J. 2013 Feb 6;32(3):424-36. doi: 10.1038/emboj.2012.348. Epub 2013 Jan 18. PMID:23334297 doi:http://dx.doi.org/10.1038/emboj.2012.348
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