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PDBsum entry 2kdg
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Structural protein
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PDB id
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2kdg
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References listed in PDB file
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Key reference
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Title
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Solution structure of the first immunoglobulin domain of human myotilin.
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Authors
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O.Heikkinen,
P.Permi,
H.Koskela,
O.Carpén,
J.Ylänne,
I.Kilpeläinen.
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Ref.
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J Biomol Nmr, 2009,
44,
107-112.
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PubMed id
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Abstract
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Myotilin is a 57 kDa actin-binding and -bundling protein that consists of a
unique serine-rich amino-terminus, two Ig-domains and a short carboxy-terminus
with a PDZ-binding motif. Myotilin localizes in sarcomeric Z-discs, where it
interacts with several sarcomeric proteins. Point mutations in myotilin cause
muscle disorders morphologically highlighted by sarcomeric disarray and
aggregation. The actin-binding and dimerization propensity of myotilin has been
mapped to the Ig-domains. Here we present high-resolution structure of the first
Ig-domain of myotilin (MyoIg1) determined with solution state NMR spectroscopy.
Nearly complete chemical shift assignments of MyoIg1 were achieved despite
several missing backbone 1H-15N-HSQC signals. The structure derived from
distance and dihedral angle restraints using torsion angle dynamics was further
refined using molecular dynamics. The structure of MyoIg1 exhibits I-type
Ig-fold. The absence of several backbone 1H-15N-HSQC signals can be explained by
conformational exchange taking place at the hydrophobic core of the protein.
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