6c9d
From Proteopedia
(Difference between revisions)
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<StructureSection load='6c9d' size='340' side='right' caption='[[6c9d]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='6c9d' size='340' side='right' caption='[[6c9d]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6c9d]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C9D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6C9D FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6c9d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C9D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6C9D FirstGlance]. <br> |
| - | </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=6c9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c9d OCA], [http://pdbe.org/6c9d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c9d RCSB], [http://www.ebi.ac.uk/pdbsum/6c9d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c9d ProSAT]</span></td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MARK1, KIAA1477, MARK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6c9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c9d OCA], [http://pdbe.org/6c9d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c9d RCSB], [http://www.ebi.ac.uk/pdbsum/6c9d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c9d ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/MARK1_HUMAN MARK1_HUMAN]] Serine/threonine-protein kinase involved in cell polarity and microtubule dynamics regulation. Phosphorylates DCX, MAP2, MAP4 and MAPT/TAU. Involved in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3).<ref>PMID:11433294</ref> <ref>PMID:17573348</ref> | [[http://www.uniprot.org/uniprot/MARK1_HUMAN MARK1_HUMAN]] Serine/threonine-protein kinase involved in cell polarity and microtubule dynamics regulation. Phosphorylates DCX, MAP2, MAP4 and MAPT/TAU. Involved in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3).<ref>PMID:11433294</ref> <ref>PMID:17573348</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The kinase associated-1 (KA1) domain is found at the C-terminus of multiple Ser/Thr protein kinases from yeast to humans, and has been assigned autoinhibitory, membrane-binding, and substrate-targeting roles. Here, we report the crystal structure of the MARK1 kinase/UBA domain bound to its autoinhibitory KA1 domain, revealing an unexpected interface at the alphaD helix and contacts with both the N- and C-lobes of the kinase domain. We confirm the binding interface location in kinetic studies of variants mutated on the kinase domain surface. Together with other MARK kinase structures, the data implicate that the KA1 domain blocks peptide substrate binding. The structure highlights the kinase-specific autoinhibitory binding modes of different KA1 domains, and provides potential new avenues by which to intervene therapeutically in Alzheimer's disease and cancers in which MARK1 or related kinases are implicated. | ||
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| + | Structural Basis for MARK1 Kinase Autoinhibition by Its KA1 Domain.,Emptage RP, Lemmon MA, Ferguson KM, Marmorstein R Structure. 2018 Aug 7;26(8):1137-1143.e3. doi: 10.1016/j.str.2018.05.008. Epub, 2018 Jun 28. PMID:30099988<ref>PMID:30099988</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6c9d" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Emptage, R P]] | [[Category: Emptage, R P]] | ||
[[Category: Marmorstein, R]] | [[Category: Marmorstein, R]] | ||
Revision as of 07:56, 29 August 2018
Crystal structure of KA1-autoinhibited MARK1 kinase
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Categories: Human | Emptage, R P | Marmorstein, R | Autoinhibition | Camkl | Ka1 domain | Kinase | Transferase
