Drug and peptide transport in humans

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<scene name='10/1066775/7pmx/1'>PepT1 is a 708-amino acid protein</scene> with an extracellular domain (beta sheets), and a transmembrane transporter domain (alpha helices) with a cytoplasmic amphipathic 2-helix linker (green protrusion). The latter looks like the '''toe of a boot''' formed by the linker (toe) with the transmembrane domain. The function of the extracellular and cytoplasmic linker domains are not well understood, although the extracellular domain appears to be important in transport<ref name="cytodom">PMID: 35580608</ref>.
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<scene name='10/1066775/7pmx/1'>PepT1 is a 708-amino acid protein</scene> with an extracellular domain (beta sheets), and a transmembrane transporter domain (alpha helices) with a cytoplasmic amphipathic linker (green protrusion). The latter looks like the '''toe of a boot''' formed by the linker (toe) with the transmembrane domain. The function of the extracellular and cytoplasmic linker domains are not well understood, although the extracellular domain appears to be important in transport<ref name="cytodom">PMID: 35580608</ref>.
The transmembrane domain has a <scene name='10/1066775/7pmx_phobic_polar/1'>predominantly hydrophobic surface</scene> (enabling it to sit within the lipid bilayer membrane) which is <scene name='10/1066775/7pmx_phobic_polar/2'>devoid of charges</scene>. The cytoplamic linker "toe" has a net positive charge, enabling it to bind to the inner leaflet of the lipid bilayer, which typically has a negative charge.
The transmembrane domain has a <scene name='10/1066775/7pmx_phobic_polar/1'>predominantly hydrophobic surface</scene> (enabling it to sit within the lipid bilayer membrane) which is <scene name='10/1066775/7pmx_phobic_polar/2'>devoid of charges</scene>. The cytoplamic linker "toe" has a net positive charge, enabling it to bind to the inner leaflet of the lipid bilayer, which typically has a negative charge.

Revision as of 04:09, 4 December 2024

This page is under construction. This notice will be removed when it is ready. Eric Martz 01:56, 3 December 2024 (UTC)

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References and Notes

  1. ↑ 1.0 1.1 1.2 1.3 1.4 Killer M, Wald J, Pieprzyk J, Marlovits TC, Low C. Structural snapshots of human PepT1 and PepT2 reveal mechanistic insights into substrate and drug transport across epithelial membranes. Sci Adv. 2021 Nov 5;7(45):eabk3259. doi: 10.1126/sciadv.abk3259. Epub 2021 Nov 3. PMID:34730990 doi:http://dx.doi.org/10.1126/sciadv.abk3259
  2. ↑ Shen J, Hu M, Fan X, Ren Z, Portioli C, Yan X, Rong M, Zhou M. Extracellular domain of PepT1 interacts with TM1 to facilitate substrate transport. Structure. 2022 Jul 7;30(7):1035-1041.e3. PMID:35580608 doi:10.1016/j.str.2022.04.011

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Eric Martz

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