Sandbox Reserved 1769: Difference between revisions
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=== Proline/Glycine Hinge === | === Proline/Glycine Hinge === | ||
<scene name='95/952697/Ntcp_open-pore_state/45'>Glycine and proline residues</scene> in the <scene name='95/952697/Ntcp_open-pore_state/43'>connecting loops</scene> and <scene name='95/952697/Ntcp_open-pore_state/42'>extra- (ECH) and intracellular helices (ICH)</scene> (Figure 3) act as hinges between the <scene name='95/952697/Ntcp_open-pore_state/44'>open pore state</scene> and <scene name='95/952697/Ntcp_inward_facing_state/5'>inward-facing states</scene> in the mechanism of bile salt uptake. This flexibility allows separation of the core and panel domains, creating a pore open to the extracellular space and exposing critical Na+ binding sites. Once substrate binds the open | <scene name='95/952697/Ntcp_open-pore_state/45'>Glycine and proline residues</scene> in the <scene name='95/952697/Ntcp_open-pore_state/43'>connecting loops</scene> and <scene name='95/952697/Ntcp_open-pore_state/42'>extra- (ECH) and intracellular helices (ICH)</scene> (Figure 3) act as hinges between the <scene name='95/952697/Ntcp_open-pore_state/44'>open pore state</scene> and <scene name='95/952697/Ntcp_inward_facing_state/5'>inward-facing states</scene> in the mechanism of bile salt uptake. This flexibility allows separation of the core and panel domains, creating a pore open to the extracellular space and exposing critical Na+ binding sites. Once substrate binds the open pore state, this hinge allows the transition to close this pore relative to the extracellular side and open to the cytoplasmic side, thus allowing release of substrate into the cell.<ref name = "Goutam" /> | ||
=== Sodium Binding Sites === | === Sodium Binding Sites === | ||
