3iz0: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 3: / Line 3: @@
 <SX load='3iz0' size='340' side='right' viewer='molstar' caption='[[3iz0]], [[Resolution|resolution]] 8.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3iz0]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IZ0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3IZ0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3iz0]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IZ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IZ0 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TA1:TAXOL'>TA1</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 8.6&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NDC80 SPC25, SPBC25, AD024 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), NUF2, RP11-77M5.2-004, SPC24 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TA1:TAXOL'>TA1</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=3iz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iz0 OCA], [http://pdbe.org/3iz0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3iz0 RCSB], [http://www.ebi.ac.uk/pdbsum/3iz0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3iz0 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=3iz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iz0 OCA], [https://pdbe.org/3iz0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3iz0 RCSB], [https://www.ebi.ac.uk/pdbsum/3iz0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3iz0 ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/TBA1B_BOVIN TBA1B_BOVIN] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.
-The Ndc80 complex is a key site of regulated kinetochore-microtubule attachment (a process required for cell division), but the molecular mechanism underlying its function remains unknown. Here we present a subnanometre-resolution cryo-electron microscopy reconstruction of the human Ndc80 complex bound to microtubules, sufficient for precise docking of crystal structures of the component proteins. We find that the Ndc80 complex binds the microtubule with a tubulin monomer repeat, recognizing alpha- and beta-tubulin at both intra- and inter-tubulin dimer interfaces in a manner that is sensitive to tubulin conformation. Furthermore, Ndc80 complexes self-associate along protofilaments through interactions mediated by the amino-terminal tail of the NDC80 protein, which is the site of phospho-regulation by Aurora B kinase. The complex's mode of interaction with the microtubule and its oligomerization suggest a mechanism by which Aurora B could regulate the stability of load-bearing kinetochore-microtubule attachments.
-The Ndc80 kinetochore complex forms oligomeric arrays along microtubules.,Alushin GM, Ramey VH, Pasqualato S, Ball DA, Grigorieff N, Musacchio A, Nogales E Nature. 2010 Oct 14;467(7317):805-10. PMID:20944740<ref>PMID:20944740</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3iz0" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Tubulin|Tubulin]]
+*[[Tubulin 3D Structures|Tubulin 3D Structures]]
-== References ==
-<references/>
 __TOC__
 </SX>
 [[Category: Bos taurus]]
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Alushin, G M]]
+[[Category: Alushin GM]]
-[[Category: Ball, D A]]
+[[Category: Ball DA]]
-[[Category: Grigorieff, N]]
+[[Category: Grigorieff N]]
-[[Category: Musacchio, A]]
+[[Category: Musacchio A]]
-[[Category: Nogales, E]]
+[[Category: Nogales E]]
-[[Category: Pasqualato, S]]
+[[Category: Pasqualato S]]
-[[Category: Ramey, V H]]
+[[Category: Ramey VH]]
-[[Category: Calponin homology domain]]
-[[Category: Cell cycle]]
-[[Category: Hec1]]
-[[Category: Kinetochore]]
-[[Category: Microtubule]]
-[[Category: Mitosis]]
-[[Category: Ndc80]]
-[[Category: Nuf2]]
-[[Category: Tubulin]]