2wb8: Difference between revisions
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<StructureSection load='2wb8' size='340' side='right'caption='[[2wb8]], [[Resolution|resolution]] 2.15Å' scene=''> | <StructureSection load='2wb8' size='340' side='right'caption='[[2wb8]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2wb8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2wb8]] is a 1 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=2WB8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WB8 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">X-ray diffraction, [[Resolution|Resolution]] 2.15Å</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=2wb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wb8 OCA], [https://pdbe.org/2wb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wb8 RCSB], [https://www.ebi.ac.uk/pdbsum/2wb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wb8 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=2wb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wb8 OCA], [https://pdbe.org/2wb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wb8 RCSB], [https://www.ebi.ac.uk/pdbsum/2wb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wb8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/HASP_HUMAN HASP_HUMAN] Serine/threonine-protein kinase that phosphorylates histone H3 at 'Ser-3' (H3T3ph) during mitosis. This positions and activates AURKB and other components of the chromosomal passenger complex (CPC) at centromeres to ensure proper chromatid cohesion, metaphase alignment and normal progression through the cell cycle.<ref>PMID:11228240</ref> <ref>PMID:15681610</ref> <ref>PMID:17084365</ref> <ref>PMID:20705812</ref> <ref>PMID:20929775</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Forneris F]] | |||
[[Category: Forneris | [[Category: Mattevi A]] | ||
[[Category: Mattevi | [[Category: Musacchio A]] | ||
[[Category: Musacchio | [[Category: Tortorci M]] | ||
[[Category: Tortorci | [[Category: Villa F]] | ||
[[Category: Villa | |||
Latest revision as of 13:10, 9 May 2024
Crystal structure of Haspin kinaseCrystal structure of Haspin kinase
Structural highlights
FunctionHASP_HUMAN Serine/threonine-protein kinase that phosphorylates histone H3 at 'Ser-3' (H3T3ph) during mitosis. This positions and activates AURKB and other components of the chromosomal passenger complex (CPC) at centromeres to ensure proper chromatid cohesion, metaphase alignment and normal progression through the cell cycle.[1] [2] [3] [4] [5] 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 PubMedHaspin, a nuclear and chromosome-associated serine/threonine (S/T) kinase, is responsible for mitotic phosphorylation of Thr-3 of histone H3. Haspin bears recognizable similarity to the eukaryotic protein kinase (ePK) fold, but its sequence is highly divergent and there is therefore considerable interest in its structural organization. We report the 2.15-A crystal structure of the kinase domain of human Haspin. The ePK fold of Haspin contains an array of insertions and deletions. The structure illustrates how Haspin escapes the classical activation scheme of most other kinases. The alphaC helix, which bears a conserved glutamate that is essential for catalysis, adopts its final active conformation within the small lobe of the kinase. It is sandwiched between an alpha-helical insertion that precedes the kinase domain, and the activation segment, which adopts an unprecedented conformation. The activation segment, which does not contain phosphorylatable residues, packs against an unusually structured alphaEF helix. Significantly extruded from the core of the fold, it forms an extensive plateau, hosting several residues implicated in substrate binding. Overall, the structure of the Haspin kinase domain reveals an active conformation that is poised for substrate recognition and phosphorylation in the absence of external regulators. Crystal structure of the catalytic domain of Haspin, an atypical kinase implicated in chromatin organization.,Villa F, Capasso P, Tortorici M, Forneris F, de Marco A, Mattevi A, Musacchio A Proc Natl Acad Sci U S A. 2009 Nov 16. PMID:19918049[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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