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==Solution structure of coiled coil domain of myosin binding subunit of myosin light chain phosphatase==
==Solution structure of coiled coil domain of myosin binding subunit of myosin light chain phosphatase==
<StructureSection load='5huz' size='340' side='right' caption='[[5huz]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='5huz' size='340' side='right'caption='[[5huz]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5huz]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HUZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HUZ FirstGlance]. <br>
<table><tr><td colspan='2'>[[5huz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2mxr 2mxr]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HUZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HUZ 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=5huz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5huz OCA], [http://pdbe.org/5huz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5huz RCSB], [http://www.ebi.ac.uk/pdbsum/5huz PDBsum]</span></td></tr>
</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=5huz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5huz OCA], [https://pdbe.org/5huz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5huz RCSB], [https://www.ebi.ac.uk/pdbsum/5huz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5huz ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/MYPT1_HUMAN MYPT1_HUMAN]] Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex, involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN-dependent suppression of HIF1A activity.<ref>PMID:19245366</ref> <ref>PMID:18477460</ref> <ref>PMID:20354225</ref>
[https://www.uniprot.org/uniprot/MYPT1_HUMAN MYPT1_HUMAN] Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex, involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN-dependent suppression of HIF1A activity.<ref>PMID:19245366</ref> <ref>PMID:18477460</ref> <ref>PMID:20354225</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Protein-protein interactions between the C-terminal domain of Myosin Binding Subunit (MBS) of MLC Phosphatase (MBS(CT180); C-terminal 180 aa) and the N-terminal coiled coil (CC) leucine zipper (LZ) domain of PKGIalpha, PKG-Ialpha(1-159) play an important role in the process of Smooth Muscle Cell relaxation. The paucity of three-dimensional structural information for MBS(CT180) prevents an atomic level understanding of the MBS-PKG contractile complex. MBS(CT180) is comprised of three structurally different sub-domains including a non-canonical CC, a CC, and a LZ. Recently we reported polypeptide purification and biophysical characterization of the CC domain and the LZ domain of MBS(CT180) (Sharma et al, Prot Expr Purif 2012). Here we report (1)H, (13)C, (15)N chemical shift assignments of homodimeric CC MBS domain encompassing amino acid residues Asp931-Leu980 using 2D and 3D heteronuclear NMR spectroscopy. Secondary structure analyses deduced from these NMR chemical shift data have identified a contiguous stretch of 36 residues from Phe932 to Ala967 that is involved in the formation of coiled coil alpha-helical region within CC MBS domain. The N-terminal residue Asp931 and the C-terminally positioned residues Thr968-Ala975, Arg977, and Ser978 adopt nonhelical loop conformations.


NMR assignment and secondary structure of coiled coil domain of C-terminal myosin binding subunit of myosin phosphatase.,Sharma AK, Rigby AC Protein Pept Lett. 2014 Jul;21(7):639-45. PMID:24693955<ref>PMID:24693955</ref>
==See Also==
 
*[[Protein phosphatase 3D structures|Protein phosphatase 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5huz" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Alper, S L]]
[[Category: Homo sapiens]]
[[Category: Anklin, C]]
[[Category: Large Structures]]
[[Category: Birrane, G]]
[[Category: Alper SL]]
[[Category: Pollak, M]]
[[Category: Anklin C]]
[[Category: Rigby, A C]]
[[Category: Birrane G]]
[[Category: Sharma, A K]]
[[Category: Pollak M]]
[[Category: Signaling protein]]
[[Category: Rigby AC]]
[[Category: Vascular smooth muscle cell]]
[[Category: Sharma AK]]
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