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PDBsum entry 5t7c
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Membrane protein
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PDB id
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5t7c
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References listed in PDB file
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Key reference
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Title
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Structure and calcium binding properties of a neuronal calcium-Myristoyl switch protein, Visinin-Like protein 3.
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Authors
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C.Li,
S.Lim,
K.H.Braunewell,
J.B.Ames.
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Ref.
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PLoS One, 2016,
11,
e0165921.
[DOI no: ]
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PubMed id
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Abstract
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Visinin-like protein 3 (VILIP-3) belongs to a family of Ca2+-myristoyl switch
proteins that regulate signal transduction in the brain and retina. Here we
analyze Ca2+ binding, characterize Ca2+-induced conformational changes, and
determine the NMR structure of myristoylated VILIP-3. Three Ca2+ bind
cooperatively to VILIP-3 at EF2, EF3 and EF4 (KD = 0.52 μM and Hill slope of
1.8). NMR assignments, mutagenesis and structural analysis indicate that the
covalently attached myristoyl group is solvent exposed in Ca2+-bound VILIP-3,
whereas Ca2+-free VILIP-3 contains a sequestered myristoyl group that interacts
with protein residues (E26, Y64, V68), which are distinct from myristate
contacts seen in other Ca2+-myristoyl switch proteins. The myristoyl group in
VILIP-3 forms an unusual L-shaped structure that places the C14 methyl group
inside a shallow protein groove, in contrast to the much deeper myristoyl
binding pockets observed for recoverin, NCS-1 and GCAP1. Thus, the myristoylated
VILIP-3 protein structure determined in this study is quite different from those
of other known myristoyl switch proteins (recoverin, NCS-1, and GCAP1). We
propose that myristoylation serves to fine tune the three-dimensional structures
of neuronal calcium sensor proteins as a means of generating functional
diversity.
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