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Article

Structure of eukaryotic purine/H(+) symporter UapA suggests a role for homodimerization in transport activity.

Nature communications - 18 Apr 2016

Alguel Yilmaz, Amillis Sotiris, Leung James, Lambrinidis George, Capaldi Stefano, Scull Nicola J, Craven Gregory, Iwata So, Armstrong Alan, Mikros Emmanuel, Diallinas George, Cameron Alexander D, Byrne Bernadette

Abstract excerpt

The uric acid/xanthine H(+) symporter, UapA, is a high-affinity purine transporter from the filamentous fungus Aspergillus nidulans. Here we present the crystal structure of a genetically stabilized version of UapA (UapA-G411VΔ1-11) in complex with xanthine. UapA is formed from two domains, a core domain and a gate domain, similar to the previously solved uracil transporter UraA, which belongs to the same family....

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Identifiers

PMID: 27088252
DOI: 10.1038/ncomms11336
PMCID: PMC4837479

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Structure of eukaryotic purine/H(+) symporter UapA suggests a role for homodimerization in transport activity.PMID 27088252Read ↗

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