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Article

Interplay between disulfide bonding and N-glycosylation defines SLC4 Na+-coupled transporter extracellular topography.

The Journal of biological chemistry - 27 Feb 2015

Zhu Quansheng, Kao Liyo, Azimov Rustam, Abuladze Natalia, Newman Debra, Kurtz Ira

Abstract excerpt

The extracellular loop 3 (EL-3) of SLC4 Na(+)-coupled transporters contains 4 highly conserved cysteines and multiple N-glycosylation consensus sites. In the electrogenic Na(+)-HCO3(-) cotransporter NBCe1-A, EL-3 is the largest extracellular loop and is predicted to consist of 82 amino acids. To determine the structural-functional importance of the conserved cysteines and the N-glycosylation sites in NBCe1-A...

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Source

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Identifiers

PMID: 25568315
DOI: 10.1074/jbc.M114.619320
PMCID: PMC4342456

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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