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5huz

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Revision as of 08:35, 10 August 2016

Solution structure of coiled coil domain of myosin binding subunit of myosin light chain phosphatase

Structural highlights

5huz is a 2 chain structure. This structure supersedes the now removed PDB entry 2mxr. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2] ^[3]

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Webb JD, Muranyi A, Pugh CW, Ratcliffe PJ, Coleman ML. MYPT1, the targeting subunit of smooth-muscle myosin phosphatase, is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH). Biochem J. 2009 May 13;420(2):327-33. doi: 10.1042/BJ20081905. PMID:19245366 doi:10.1042/BJ20081905
↑ Yamashiro S, Yamakita Y, Totsukawa G, Goto H, Kaibuchi K, Ito M, Hartshorne DJ, Matsumura F. Myosin phosphatase-targeting subunit 1 regulates mitosis by antagonizing polo-like kinase 1. Dev Cell. 2008 May;14(5):787-97. doi: 10.1016/j.devcel.2008.02.013. PMID:18477460 doi:10.1016/j.devcel.2008.02.013
↑ Zagorska A, Deak M, Campbell DG, Banerjee S, Hirano M, Aizawa S, Prescott AR, Alessi DR. New roles for the LKB1-NUAK pathway in controlling myosin phosphatase complexes and cell adhesion. Sci Signal. 2010 Mar 30;3(115):ra25. doi: 10.1126/scisignal.2000616. PMID:20354225 doi:http://dx.doi.org/10.1126/scisignal.2000616
↑ Sharma AK, Rigby AC. NMR assignment and secondary structure of coiled coil domain of C-terminal myosin binding subunit of myosin phosphatase. Protein Pept Lett. 2014 Jul;21(7):639-45. PMID:24693955

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5huz"

@@ Line 3: / Line 3: @@
 <StructureSection load='5huz' size='340' side='right' caption='[[5huz]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == 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. 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 [http://oca.weizmann.ac.il/oca-docs/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'>[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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5huz ProSAT]</span></td></tr>
 </table>
 == Function ==

5huz

From Proteopedia

Revision as of 08:35, 10 August 2016

Solution structure of coiled coil domain of myosin binding subunit of myosin light chain phosphatase

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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