Myosin light chain kinase

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{{STRUCTURE_2x4f| PDB=2x4f | SIZE=400| SCENE= |right|CAPTION=Two monomers of human myosin light chain kinase residues 40-388 complex with pyrimidine derivative, pentaethylene glycol, ethanediol and sulfate ion, [[2x4f]] }}
{{STRUCTURE_2x4f| PDB=2x4f | SIZE=400| SCENE= |right|CAPTION=Two monomers of human myosin light chain kinase residues 40-388 complex with pyrimidine derivative, pentaethylene glycol, ethanediol and sulfate ion, [[2x4f]] }}
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'''Myosin light chain kinase''' (MLCK) phosphorylates the regulatory light chain of myosin at serine residue 19. This phosphorylation enables the myosin crossbridge to bind to the actin filament and allows muscle contraction to begin. Dephosphorylation of the myosin light chain stops muscle contraction<ref>PMID:7935354</ref>.
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'''Myosin light chain kinase''' (MLCK) phosphorylates the regulatory light chain of myosin at serine residue 19. This phosphorylation enables the myosin crossbridge to bind to the actin filament and allow muscle contraction to begin. Dephosphorylation of the myosin light chain stops muscle contraction.
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==3D structures of MLCK==
==3D structures of MLCK==
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[[2x4f]] – hMLCK residues 40-388
[[2x4f]] – hMLCK residues 40-388
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 06:54, 4 May 2016

Template:STRUCTURE 2x4f


Myosin light chain kinase (MLCK) phosphorylates the regulatory light chain of myosin at serine residue 19. This phosphorylation enables the myosin crossbridge to bind to the actin filament and allows muscle contraction to begin. Dephosphorylation of the myosin light chain stops muscle contraction[1].

3D structures of MLCK

2cqv – hMLCK 8th Ig-like domain – human – NMR
2yr3 - hMLCK 4th Ig-like domain – NMR
2x4f – hMLCK residues 40-388

References

  1. ↑ Stull JT, Tansey MG, Tang DC, Word RA, Kamm KE. Phosphorylation of myosin light chain kinase: a cellular mechanism for Ca2+ desensitization. Mol Cell Biochem. 1993 Nov;127-128:229-37. PMID:7935354

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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