6mky

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'''Unreleased structure'''
 
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The entry 6mky is ON HOLD until Paper Publication
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==Human SDS22==
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<StructureSection load='6mky' size='340' side='right' caption='[[6mky]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6mky]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MKY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MKY FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<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=6mky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mky OCA], [http://pdbe.org/6mky PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mky RCSB], [http://www.ebi.ac.uk/pdbsum/6mky PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mky ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/PP1R7_HUMAN PP1R7_HUMAN]] Regulatory subunit of protein phosphatase 1.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Protein phosphatase 1 (PP1) dephosphorylates hundreds of key biological targets by associating with nearly 200 regulatory proteins to form highly specific holoenzymes. The vast majority of regulators are intrinsically disordered proteins (IDPs) and bind PP1 via short linear motifs within their intrinsically disordered regions. One of the most ancient PP1 regulators is SDS22, a protein that is conserved from yeast to mammals. Sequence analysis of SDS22 revealed that it is a leucine-rich repeat (LRR) protein, suggesting that SDS22, unlike nearly every other known PP1 regulator, is not an IDP but instead is fully structured. Here, the 2.9 A resolution crystal structure of human SDS22 in space group P212121 is reported. SDS22 adopts an LRR fold with the horseshoe-like curvature typical for this family of proteins. The structure results in surfaces with distinct chemical characteristics that are likely to be critical for PP1 binding.
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Authors: Choy, M.S., Bolik-Coulon, N., Page, R., Peti, W.
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The structure of SDS22 provides insights into the mechanism of heterodimer formation with PP1.,Choy MS, Bolik-Coulon N, Archuleta TL, Peti W, Page R Acta Crystallogr F Struct Biol Commun. 2018 Dec 1;74(Pt 12):817-824. doi:, 10.1107/S2053230X18016503. Epub 2018 Nov 30. PMID:30511677<ref>PMID:30511677</ref>
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Description: Human SDS22
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6mky" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Bolik-Coulon, N]]
[[Category: Bolik-Coulon, N]]
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[[Category: Peti, W]]
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[[Category: Choy, M S]]
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[[Category: Choy, M.S]]
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[[Category: Page, R]]
[[Category: Page, R]]
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[[Category: Peti, W]]
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[[Category: Cell cycle]]
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[[Category: Lrr repeat]]
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[[Category: Pp1]]
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[[Category: Sds22]]
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[[Category: Signaling protein]]

Revision as of 06:57, 12 December 2018

Human SDS22

6mky, resolution 2.90Å

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