4c9y: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4c9y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C9Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C9Y FirstGlance]. <br> | <table><tr><td colspan='2'>[[4c9y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C9Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C9Y FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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]] 2.01Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4c9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c9y OCA], [https://pdbe.org/4c9y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c9y RCSB], [https://www.ebi.ac.uk/pdbsum/4c9y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c9y ProSAT]</span></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=4c9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c9y OCA], [https://pdbe.org/4c9y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c9y RCSB], [https://www.ebi.ac.uk/pdbsum/4c9y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c9y ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | |||
The ability of kinetochores (KTs) to maintain stable attachments to dynamic microtubule structures ('straight' during microtubule polymerization and 'curved' during microtubule depolymerization) is an essential requirement for accurate chromosome segregation. Here we show that the kinetochore-associated Ska complex interacts with tubulin monomers via the carboxy-terminal winged-helix domain of Ska1, providing the structural basis for the ability to bind both straight and curved microtubule structures. This contrasts with the Ndc80 complex, which binds straight microtubules by recognizing the dimeric interface of tubulin. The Ska1 microtubule-binding domain interacts with tubulins using multiple contact sites that allow the Ska complex to bind microtubules in multiple modes. Disrupting either the flexibility or the tubulin contact sites of the Ska1 microtubule-binding domain perturbs normal mitotic progression, explaining the critical role of the Ska complex in maintaining a firm grip on dynamic microtubules. | |||
Structural basis for microtubule recognition by the human kinetochore Ska complex.,Abad MA, Medina B, Santamaria A, Zou J, Plasberg-Hill C, Madhumalar A, Jayachandran U, Redli PM, Rappsilber J, Nigg EA, Jeyaprakash AA Nat Commun. 2014 Jan 13;5:2964. doi: 10.1038/ncomms3964. PMID:24413531<ref>PMID:24413531</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4c9y" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Latest revision as of 05:44, 21 November 2024
Structural Basis for the microtubule binding of the human kinetochore Ska complexStructural Basis for the microtubule binding of the human kinetochore Ska complex
Structural highlights
Publication Abstract from PubMedThe ability of kinetochores (KTs) to maintain stable attachments to dynamic microtubule structures ('straight' during microtubule polymerization and 'curved' during microtubule depolymerization) is an essential requirement for accurate chromosome segregation. Here we show that the kinetochore-associated Ska complex interacts with tubulin monomers via the carboxy-terminal winged-helix domain of Ska1, providing the structural basis for the ability to bind both straight and curved microtubule structures. This contrasts with the Ndc80 complex, which binds straight microtubules by recognizing the dimeric interface of tubulin. The Ska1 microtubule-binding domain interacts with tubulins using multiple contact sites that allow the Ska complex to bind microtubules in multiple modes. Disrupting either the flexibility or the tubulin contact sites of the Ska1 microtubule-binding domain perturbs normal mitotic progression, explaining the critical role of the Ska complex in maintaining a firm grip on dynamic microtubules. Structural basis for microtubule recognition by the human kinetochore Ska complex.,Abad MA, Medina B, Santamaria A, Zou J, Plasberg-Hill C, Madhumalar A, Jayachandran U, Redli PM, Rappsilber J, Nigg EA, Jeyaprakash AA Nat Commun. 2014 Jan 13;5:2964. doi: 10.1038/ncomms3964. PMID:24413531[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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