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

Structural insights into the binding of nanobodies LaM2 and LaM4 to the red fluorescent protein mCherry.

Protein science : a publication of the Protein Society - 1 Nov 2021

Wang Ziying, Li Long, Hu Rongting, Zhong Peiyu, Zhang Yiran, Cheng Shihao, Jiang He, Liu Rui, Ding Yu

Abstract excerpt

Red fluorescent proteins (RFPs) are powerful tools used in molecular biology research. Although RFP can be easily monitored in vivo, manipulation of RFP by suitable nanobodies binding to different epitopes of RFP is still desired. Thus, it is crucial to obtain structural information on how the different nanobodies interact with RFP. Here, we determined the crystal structures of the LaM2-mCherry and LaM4-mCherry...

Read the complete abstract on PubMed

Topics

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

Share to Luminescent Proteins
Share to Mutation

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Protein Domains

Share to Protein Structure, Secondary

Share to Recombinant Fusion Proteins

Share to Red Fluorescent Protein

Share to Single-Domain Antibodies

Source

Open in PubMed Open full text

Identifiers

PMID: 34562299
DOI: 10.1002/pro.4194
PMCID: PMC8521304

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural insights into the binding of nanobodies LaM2 and LaM4 to the red fluorescent protein mCherry.PMID 34562299Read ↗

Peptides in headlock--a novel high-affinity and versatile peptide-binding nanobody for proteomics and microscopy.Semantic proximity Read ↗

Generation of longer emission wavelength red fluorescent proteins using computationally designed libraries.Semantic proximity Read ↗

Rational design of a monomeric and photostable far-red fluorescent protein for fluorescence imaging in vivo.Semantic proximity Read ↗

Oligomerization-Dependent Regulation of LrhA Controls Bacterial Flagellar Biosynthesis.Semantic proximity Read ↗

Structural insights in the GTP-driven monomerization and activation of a bacterial LRRK2 homologue using allosteric nanobodiesSemantic proximity Read ↗

TR-FRET assays of Huntingtin protein fragments reveal temperature and polyQ length-dependent conformational changes.Semantic proximity Read ↗

A Very Bright Far-Red Bioluminescence Emitting Combination Based on Engineered Railroad Worm Luciferase and 6'-Amino-Analogs for Bioimaging Purposes.Semantic proximity Read ↗

Metal ions-binding T4 lysozyme as an intramolecular protein purification tag compatible with X-ray crystallography.Semantic proximity Read ↗

Boosting the toolbox for live imaging of translationSemantic proximity Read ↗

Mutagenesis of mNeptune Red-Shifts Emission Spectrum to 681-685 nm.Semantic proximity Read ↗

A naturally monomeric infrared fluorescent protein for protein labeling in vivo.Semantic proximity Read ↗

Design of Light-Controlled Protein Conformations and Functions.Semantic proximity Read ↗

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