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PDBsum entry 5k6p
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Contractile protein
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PDB id
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5k6p
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References listed in PDB file
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Key reference
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Title
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A highly conserved yet flexible linker is part of a polymorphic protein-Binding domain in myosin-Binding protein c.
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Authors
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K.A.Michie,
A.H.Kwan,
C.S.Tung,
J.M.Guss,
J.Trewhella.
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Ref.
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Structure, 2016,
24,
2000-2007.
[DOI no: ]
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PubMed id
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Abstract
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The nuclear magnetic resonance (NMR) structure of the tri-helix bundle (THB) of
the m-domain plus C2 (ΔmC2) of myosin-binding protein C (MyBP-C) has revealed a
highly flexible seven-residue linker between the structured THB and C2.
Bioinformatics shows significant patterns of conservation across the THB-linker
sequence, with the linker containing a strictly conserved serine in all MyBP-C
isoforms. Clinically linked mutations further support the functional
significance of the THB-linker region. NMR, small-angle X-ray scattering, and
binding studies show the THB-linker plus the first ten residues of C2 undergo
dramatic changes when ΔmC2 binds Ca2+-calmodulin, with the linker
and C2 N-terminal residues contributing significantly to the affinity. Modeling
of all available experimental data indicates that the THB tertiary structure
must be disrupted to form the complex. These results are discussed in the
context of the THB-linker and the N-terminal residues of C2 forming a
polymorphic binding domain that could accommodate multiple binding partners in
the dynamic sarcomere.
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