3vza: Difference between revisions
No edit summary |
No edit summary |
||
| (4 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Crystal structure of the chicken Spc24-Spc25 globular domain in complex with CENP-T peptide== | |||
<StructureSection load='3vza' size='340' side='right'caption='[[3vza]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3vza]] is a 6 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=3VZA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VZA FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.898Å</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=3vza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vza OCA], [https://pdbe.org/3vza PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vza RCSB], [https://www.ebi.ac.uk/pdbsum/3vza PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vza ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/E1C4Y2_CHICK E1C4Y2_CHICK] | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:23334297</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3vza" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Centromere protein 3D structure|Centromere protein 3D structure]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Gallus gallus]] | |||
[[Category: Large Structures]] | |||
[[Category: Fukagawa T]] | |||
[[Category: Nishino T]] | |||
Latest revision as of 15:42, 8 November 2023
Crystal structure of the chicken Spc24-Spc25 globular domain in complex with CENP-T peptideCrystal structure of the chicken Spc24-Spc25 globular domain in complex with CENP-T peptide
Structural highlights
FunctionPublication Abstract from PubMedThe 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. See AlsoReferences
|
| ||||||||||||||||