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Article

Two perfectly conserved arginine residues are required for substrate binding in a high-affinity nitrate transporter.

Proceedings of the National Academy of Sciences of the United States of America - 14 Dec 2004

Unkles Shiela E, Rouch Duncan A, Wang Ye, Siddiqi M Yaeesh, Glass Anthony D M, Kinghorn James R

Abstract excerpt

This study represents the first attempt to investigate the molecular mechanisms by which nitrate, an anion of significant ecological, agricultural, and medical importance, is transported into cells by high-affinity nitrate transporters. Two charged residues, R87 and R368, located within hydrophobic transmembrane domains 2 and 8, respectively, are conserved in all 52 high-affinity nitrate transporters sequenced...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 15576512
DOI: 10.1073/pnas.0405054101
PMCID: PMC536016

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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