ArticlePharmaceutical research1997
Sequence alignments of the H(+)-dependent oligopeptide transporter family PTR: inferences on structure and function of the intestinal PET1 transporter.
Article in Pharmaceutical research, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 21 citations in OpenAlex.
- Alternative Splicing: Expanding Diversity in Major ABC and SLC Drug Transporters.The AAPS journal · 2017Review
- ABC and SLC transporter expression and proton oligopeptide transporter (POT) mediated permeation across the human blood--brain barrier cell line, hCMEC/D3 [corrected].Molecular pharmaceutics · 2010Article
- Comparative analysis of vertebrate PEPT1 and PEPT2 genes.Genetica · 2010Article
- Harnessing natural diversity to probe metabolic pathways.PLoS genetics · 2005Article
- Molecular and developmental biology of inorganic nitrogen nutrition.The arabidopsis book · 2002Article
- Spatial expression patterns of peptide transporters in the human and rat gastrointestinal tracts, Caco-2 in vitro cell culture model, and multiple human tissues.AAPS pharmSci · 2001Article
- Genomic structure of proton-coupled oligopeptide transporter hPEPT1 and pH-sensing regulatory splice variant.AAPS pharmSci · 2001Article
- Human proton/oligopeptide transporter (POT) genes: identification of putative human genes using bioinformatics.AAPS pharmSci · 2000Article
- Intestinal peptide transport systems and oral drug availability.Pharmaceutical research · 1999Review
- The Venus flytrap of periplasmic binding proteins: an ancient protein module present in multiple drug receptors.AAPS pharmSci · 1999Review
- Evolutionary relationships among proteins probed by an iterative neighborhood cluster analysis (INCA). Alignment of bacteriorhodopsins with the yeast sequence YRO2.Pharmaceutical research · 1997Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
purposeTo study the structure and function of the intestinal H+/ peptide transporter PET1, we compared its amino acid sequence with those of related transporters belonging to the oligopeptide transporter family PTR, and with more distant transporter families.
methodsWe have developed a new approach to the sequence analysis of proteins with multiple transmembrane domains (TMDs) which takes into account the repeated TMD-loop topology. In addition to conventional analyses of the entire sequence, each TMD and its adjacent loop residues (= TMD segments) were analyzed separately as independent structural units. In combination with hydropathy analysis, this approach reveals any changes in the order of the TMD segments in the primary structure and permits TMD alignments among divergent structures even if rearrangements of the order of TMD segments have occurred in the course of evolution.
resultsAlignments of TMD segments indicate that the TMD order in PTR transporters may have changed in the process of evolution. Consideration of such changes permits the alignment of homologous TMD segments from PTR transporters belonging to distant akaryotic and eukaryotic phyla. Multiple alignments of TMDs reveal several highly conserved regions that may play a role in transporter function. In comparing the PTR transporters with other transporter gene families, alignment scores using the entire primary structure are too low to support a finding of probable homology. However, statistically significant alignments were observed among individual TMD segments if one disregards the order in which they occur in the primary structure.
conclusionsOur results support the hypothesis that the PTR transporters may have evolved by rearrangement, duplication, or insertions and deletions of TMD segments as independent modules. This modular structure suggests new alignment strategies for determining functional domains and testing relationship among distant transporter families.
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