Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Requirement for asparagine in the aquaporin NPA sequence signature motifs for cation exclusion

15 Dec 2010

Abstract excerpt

Two highly conserved NPA motifs are a hallmark of the aquaporin (AQP) family. The NPA triplets form N-terminal helix capping structures with the Asn side chains located in the centre of the water or solute-conducting channel, and are considered to play an important role in AQP selectivity. Although another AQP selectivity filter site, the aromatic/Arg (ar/R) constriction, has been well characterized by mutational...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cystic Fibrosis Research Advances
Share to Ion Transport and Channel Regulation

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 21205205
DOI: 10.1111/j.1742-4658.2010.07993.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Requirement for asparagine in the aquaporin NPA sequence signature motifs for cation exclusionPMID 21205205Read ↗

Electrostatics of aquaporin and aquaglyceroporin channels correlates with their transport selectivity.Semantic proximity Read ↗

Voltage-gated sodium channel (NaV) protein dissection creates a set of functional pore-only proteins.Semantic proximity Read ↗

The hidden intricacies of aquaporins: Remarkable details in a common structural scaffoldSemantic proximity Read ↗

Analysis of conserved NCS2 motifs in the Escherichia coli xanthine permease XanQ.Semantic proximity Read ↗

Towards Molecular Understanding of the pH Dependence Characterizing NhaA of Which Structural Fold is Shared by Other Transporters.Semantic proximity Read ↗

A CLAG3 mutation in an amphipathic transmembrane domain alters malaria parasite nutrient channels and confers leupeptin resistance.Semantic proximity Read ↗

Site-directed mutations reflecting functional and structural properties of Ec-NhaA.Semantic proximity Read ↗

Alanine scanning mutagenesis of a high-affinity nitrate transporter highlights the requirement for glycine and asparagine residues in the two nitrate signature motifs.Semantic proximity Read ↗

A cationic lipid site at the outward transmembrane face of a pentameric ligand-gated ion channelSemantic proximity Read ↗

The contact region between three domains of the extracellular loop of ASIC1a is critical for channel function.Semantic proximity Read ↗

A conserved asparagine in a P-type proton pump is required for efficient gating of protons.Semantic proximity Read ↗

Molecular basis of ion permeability in a voltage-gated sodium channel.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.