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基本情報
登録情報 | ![]() |
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![]() | Cardiac myosin binding protein-C: domains C5-C6-C7
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機能・相同性 | ![]() C zone / regulation of muscle filament sliding / striated muscle myosin thick filament / regulation of striated muscle contraction / cardiac myofibril / positive regulation of ATP-dependent activity / Striated Muscle Contraction / M band / A band / structural constituent of muscle ...C zone / regulation of muscle filament sliding / striated muscle myosin thick filament / regulation of striated muscle contraction / cardiac myofibril / positive regulation of ATP-dependent activity / Striated Muscle Contraction / M band / A band / structural constituent of muscle / sarcomere organization / ventricular cardiac muscle tissue morphogenesis / myosin heavy chain binding / myosin binding / ATPase activator activity / heart morphogenesis / cardiac muscle contraction / titin binding / sarcomere / actin binding / cell adhesion / metal ion binding / identical protein binding / cytosol 類似検索 - 分子機能 |
生物種 | ![]() |
![]() | ![]() タイトル: Clinically Linked Mutations in the Central Domains of Cardiac Myosin-Binding Protein C with Distinct Phenotypes Show Differential Structural Effects. 著者: Naveed Ahmed Nadvi / Katharine A Michie / Ann H Kwan / J Mitchell Guss / Jill Trewhella / ![]() 要旨: The structural effects of three missense mutations clinically linked to hypertrophic cardiomyopathy (HCM) and located in the central domains of cardiac myosin-binding protein C (cMyBP-C) have been ...The structural effects of three missense mutations clinically linked to hypertrophic cardiomyopathy (HCM) and located in the central domains of cardiac myosin-binding protein C (cMyBP-C) have been determined using small-angle scattering, infrared spectroscopy, and nuclear magnetic resonance spectroscopy. Bioinformatics and modeling were used to initially predict the expected structural impacts and assess the broader implications for function based on sequence conservation patterns. The experimental results generally affirm the predictions that two of the mutations (D745G, P873H) disrupt domain folding, while the third (R820Q) is likely to be entirely solvent exposed and thus more likely to have its impact through its interactions within the sarcomere. Each of the mutations is associated with distinct disease phenotypes, with respect to severity, stage of onset, and end phase. The results are discussed in terms of understanding key structural features of these domains essential for healthy function and the role they may play in disease development. |
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構造の表示
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-モデル
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試料
![]() | 名称: Cardiac myosin binding protein-C: domains C5-C6-C7 / 試料濃度: 0.70-3.40 |
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バッファ | 名称: 25 mM Tris-HCl, 250 mM NaCl, 2 mM TCEP, 0.02% sodium azide 濃度: 25.00 mM / pH: 7.5 / 組成: 250 mM NaCl, 2 mM TCEP, 0.02% sodium azide |
要素 #352 | 名称: cMyBP-C / タイプ: protein / 記述: Cardiac myosin binding protein-C: domains C5-C6-C7 / 分子量: 35.751 / 分子数: 1 / 由来: Homo sapiens / 参照: UniProt: Q14896 配列: GPGSRQEPPK IHLDCPGRIP DTIVVVAGNK LRLDVPISGD PAPTVIWQKA ITQGNKAPAR PAPDAPEDTG DSDEWVFDKK LLCETEGRVR VETTKDRSIF TVEGAEKEDE GVYTVTVKNP VGEDQVNLTV KVIDVPDAPA APKISNVGED SCTVQWEPPA YDGGQPILGY ...配列: GPGSRQEPPK IHLDCPGRIP DTIVVVAGNK LRLDVPISGD PAPTVIWQKA ITQGNKAPAR PAPDAPEDTG DSDEWVFDKK LLCETEGRVR VETTKDRSIF TVEGAEKEDE GVYTVTVKNP VGEDQVNLTV KVIDVPDAPA APKISNVGED SCTVQWEPPA YDGGQPILGY ILERKKKKSY RWMRLNFDLI QELSHEARRM IEGVVYEMRV YAVNAIGMSR PSPASQPFMP IGPPSEPTHL AVEDVSDTTV SLKWRPPERV GAGGLDGYSV EYCPEGCSEW VAALQGLTEH TSILVKDLPT GARLLFRVRA HNMAGPGAPV TTTEPVTV |
-実験情報
ビーム | 設備名称: Australian Synchrotron SAXS/WAXS / 地域: Melbourne / 国: Australia ![]() | |||||||||||||||||||||||||||||||||
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検出器 | 名称: Pilatus 1M | |||||||||||||||||||||||||||||||||
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距離分布関数 P(R) |
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