2aff: Difference between revisions
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==The solution structure of the Ki67FHA/hNIFK(226-269)3P complex== | ==The solution structure of the Ki67FHA/hNIFK(226-269)3P complex== | ||
<StructureSection load='2aff' size='340' side='right' caption='[[2aff | <StructureSection load='2aff' size='340' side='right'caption='[[2aff]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2aff]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2aff]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AFF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AFF FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 100 models</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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=2aff FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aff OCA], [https://pdbe.org/2aff PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aff RCSB], [https://www.ebi.ac.uk/pdbsum/2aff PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aff ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/KI67_HUMAN KI67_HUMAN] Thought to be required for maintaining cell proliferation. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/af/2aff_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/af/2aff_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| Line 35: | Line 33: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Byeon | [[Category: Large Structures]] | ||
[[Category: Gronenborn | [[Category: Byeon I-JL]] | ||
[[Category: Li | [[Category: Gronenborn AM]] | ||
[[Category: Song | [[Category: Li H]] | ||
[[Category: Tsai | [[Category: Song H]] | ||
[[Category: Tsai MD]] | |||
Latest revision as of 10:48, 30 October 2024
The solution structure of the Ki67FHA/hNIFK(226-269)3P complexThe solution structure of the Ki67FHA/hNIFK(226-269)3P complex
Structural highlights
FunctionKI67_HUMAN Thought to be required for maintaining cell proliferation. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe forkhead-associated (FHA) domain of human Ki67 interacts with the human nucleolar protein hNIFK, recognizing a 44-residue fragment, hNIFK226-269, phosphorylated at Thr234. Here we show that high-affinity binding requires sequential phosphorylation by two kinases, CDK1 and GSK3, yielding pThr238, pThr234 and pSer230. We have determined the solution structure of Ki67FHA in complex with the triply phosphorylated peptide hNIFK226-269(3P), revealing not only local recognition of pThr234 but also the extension of the beta-sheet of the FHA domain by the addition of a beta-strand of hNIFK. The structure of an FHA domain in complex with a biologically relevant binding partner provides insights into ligand specificity and potentially links the cancer marker protein Ki67 to a signaling pathway associated with cell fate specification. Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67.,Byeon IJ, Li H, Song H, Gronenborn AM, Tsai MD Nat Struct Mol Biol. 2005 Nov;12(11):987-93. PMID:16244663[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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