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Article

Outward-facing conformers of LacY stabilized by nanobodies.

Proceedings of the National Academy of Sciences of the United States of America - 30 Dec 2014

Smirnova Irina, Kasho Vladimir, Jiang Xiaoxu, Pardon Els, Steyaert Jan, Kaback H Ronald

Abstract excerpt

The lactose permease of Escherichia coli (LacY), a highly dynamic polytopic membrane protein, catalyzes stoichiometric galactoside/H(+) symport by an alternating access mechanism and exhibits multiple conformations, the distribution of which is altered by sugar binding. We have developed single-domain camelid nanobodies (Nbs) against a LacY mutant in an outward (periplasmic)-open conformation to stabilize this...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 25512549
DOI: 10.1073/pnas.1422265112
PMCID: PMC4284591

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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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