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{{STRUCTURE_3vza|  PDB=3vza  |  SCENE=  }}
===Crystal structure of the chicken Spc24-Spc25 globular domain in complex with CENP-T peptide===
{{ABSTRACT_PUBMED_23334297}}


==Function==
==Crystal structure of the chicken Spc24-Spc25 globular domain in complex with CENP-T peptide==
[[http://www.uniprot.org/uniprot/CENPT_CHICK CENPT_CHICK]] Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation (By similarity). The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres (By similarity). Part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENPT has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis.<ref>PMID:19070575</ref> <ref>PMID:22304917</ref> 
<StructureSection load='3vza' size='340' side='right'caption='[[3vza]], [[Resolution|resolution]] 1.90&Aring;' 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]] 1.898&#8491;</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.


==About this Structure==
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>
[[3vza]] is a 6 chain structure with sequence from [http://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].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
<references group="xtra"/><references/>
</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: 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]]

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

3vza is a 6 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.898Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

See Also

References

  1. ↑ 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

3vza, resolution 1.90Å

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