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基本情報
登録情報 | データベース: PDB / ID: 8tk8 | ||||||||||||
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タイトル | Human Type 3 IP3 Receptor - Resting State (+IP3/ATP) | ||||||||||||
![]() | Inositol 1,4,5-trisphosphate receptor type 3 | ||||||||||||
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機能・相同性 | ![]() sensory perception of bitter taste / DAG and IP3 signaling / sensory perception of umami taste / inositol 1,3,4,5 tetrakisphosphate binding / inositol 1,4,5-trisphosphate-gated calcium channel activity / sensory perception of sweet taste / platelet dense tubular network membrane / Elevation of cytosolic Ca2+ levels / Effects of PIP2 hydrolysis / PLC beta mediated events ...sensory perception of bitter taste / DAG and IP3 signaling / sensory perception of umami taste / inositol 1,3,4,5 tetrakisphosphate binding / inositol 1,4,5-trisphosphate-gated calcium channel activity / sensory perception of sweet taste / platelet dense tubular network membrane / Elevation of cytosolic Ca2+ levels / Effects of PIP2 hydrolysis / PLC beta mediated events / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() 類似検索 - 分子機能 | ||||||||||||
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![]() | Paknejad, N. / Sapuru, V. / Hite, R.K. | ||||||||||||
資金援助 | ![]()
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![]() | ![]() タイトル: Structural titration reveals Ca-dependent conformational landscape of the IP receptor. 著者: Navid Paknejad / Vinay Sapuru / Richard K Hite / ![]() 要旨: Inositol 1,4,5-trisphosphate receptors (IPRs) are endoplasmic reticulum Ca channels whose biphasic dependence on cytosolic Ca gives rise to Ca oscillations that regulate fertilization, cell division ...Inositol 1,4,5-trisphosphate receptors (IPRs) are endoplasmic reticulum Ca channels whose biphasic dependence on cytosolic Ca gives rise to Ca oscillations that regulate fertilization, cell division and cell death. Despite the critical roles of IPR-mediated Ca responses, the structural underpinnings of the biphasic Ca dependence that underlies Ca oscillations are incompletely understood. Here, we collect cryo-EM images of an IPR with Ca concentrations spanning five orders of magnitude. Unbiased image analysis reveals that Ca binding does not explicitly induce conformational changes but rather biases a complex conformational landscape consisting of resting, preactivated, activated, and inhibited states. Using particle counts as a proxy for relative conformational free energy, we demonstrate that Ca binding at a high-affinity site allows IPRs to activate by escaping a low-energy resting state through an ensemble of preactivated states. At high Ca concentrations, IPRs preferentially enter an inhibited state stabilized by a second, low-affinity Ca binding site. Together, these studies provide a mechanistic basis for the biphasic Ca-dependence of IPR channel activity. | ||||||||||||
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PDBx/mmCIF形式 | ![]() | 4.2 MB | 表示 | ![]() |
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-関連構造データ
関連構造データ | ![]() 41323MC ![]() 8tkdC ![]() 8tkeC ![]() 8tkfC ![]() 8tkgC ![]() 8tkhC ![]() 8tkiC ![]() 8tl9C ![]() 8tlaC M: このデータのモデリングに利用したマップデータ C: 同じ文献を引用 ( |
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類似構造データ | 類似検索 - 機能・相同性 ![]() |
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非結晶学的対称性 (NCS) | NCSドメイン:
NCSドメイン領域: Ens-ID: ens_1
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