Sandbox Reserved 1794: Difference between revisions
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=== Overview === | === Overview === | ||
NTCP is one continuous polypeptide chain containing <scene name='95/952722/Labeled_9_helices/5'>9 transmembrane alpha helices</scene>. The N-terminus of the polypeptide chain | NTCP is one continuous polypeptide chain containing <scene name='95/952722/Labeled_9_helices/5'>9 transmembrane alpha helices</scene>.<ref name="Goutam"/> The N-terminus of the polypeptide chain extrudes into the extracellular region of the plasma membrane while the C-terminus juts into the intracellular region. NTCP contains <scene name='95/952722/Ntcp_core_domain-_blue/9'>Two distinct sub domains</scene>: a core domain and a panel domain, which together channel opening and bile salt transport (Fig. 2). The <scene name='95/952722/Ntcp_core_domain-_blue/8'>core domain</scene> <font color='#6060ff'><b>(blue)</b></font> contains 6 transmembrane α helices (TM2-4 and TM7-9) and demonstrates [https://en.wikipedia.org/wiki/Protein_structure two-fold pseudosymmetry]. The <scene name='95/952722/Ntcp_panel_domain-_red/4'>panel domain</scene> <font color='red'><b>(red)</b></font> consists of 3 transmembrane α helices (TM1 and TM5-6) and is asymmetrical. Within the core domain, a unique crossover between TM-3 and TM-8 creates an <scene name='95/952722/Ntcp_x_motif/8'>X motif</scene>. The X motif contains the substrate binding site required for transport and essential residues for the conformational change required for transport. The core and panel domains are also connected by both extracellular and intracellular <scene name='95/952722/Connector_helices/5'>connector helices</scene> that are separate from the nine transmembrane α helices. | ||