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-Structure paper
タイトル | A Highly Conserved Yet Flexible Linker Is Part of a Polymorphic Protein-Binding Domain in Myosin-Binding Protein C. |
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ジャーナル・号・ページ | Structure, Vol. 24, Issue 11, Page 2000-2007, Year 2016 |
掲載日 | 2016年11月1日 |
![]() | Katharine A Michie / Ann H Kwan / Chang-Shung Tung / J Mitchell Guss / Jill Trewhella / ![]() ![]() |
PubMed 要旨 | 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 ...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 Ca-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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手法 | SAS (X-ray synchrotron) / NMR (溶液) |
構造データ | ![]() SASDDD9: ![]() PDB-5k6p: |
由来 |
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![]() | CONTRACTILE PROTEIN / immunoglobulin |