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

Crystal structure of a thermally stable rhodopsin mutant.

Journal of molecular biology - 5 Oct 2007

Standfuss Jörg, Xie Guifu, Edwards Patricia C, Burghammer Manfred, Oprian Daniel D, Schertler Gebhard F X

Abstract excerpt

We determined the structure of the rhodopsin mutant N2C/D282C expressed in mammalian cells; the first structure of a recombinantly produced G protein-coupled receptor (GPCR). The mutant was designed to form a disulfide bond between the N terminus and loop E3, which allows handling of opsin in detergent solution and increases thermal stability of rhodopsin by 10 deg.C. It allowed us to crystallize a fully...

Read the complete abstract on PubMed

Topics

Animals
COS Cells
Cattle
Chlorocebus aethiops
Crystallography, X-Ray
Disulfides
Humans

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

Models, Molecular

Molecular Sequence Data

Mutant Proteins

Mutation

Protein Structure, Tertiary

Recombinant Proteins

Rhodopsin

Temperature

Source

Open in PubMed Open full text

Identifiers

PMID: 17825322
DOI: 10.1016/j.jmb.2007.03.007
PMCID: PMC2258155

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Crystal structure of a thermally stable rhodopsin mutant.PMID 17825322Read ↗

A crystal clear solution for determining G-protein-coupled receptor structures.Semantic proximity Read ↗

Conformational thermostabilization of the beta1-adrenergic receptor in a detergent-resistant form.Semantic proximity Read ↗

Highly conserved tyrosine stabilizes the active state of rhodopsin.Semantic proximity Read ↗

Systematic profiling of temperature- and retinal-sensitive rhodopsin variants by deep mutational scanning.Semantic proximity Read ↗

Structure and function in rhodopsin. Separation and characterization of the correctly folded and misfolded opsins produced on expression of an opsin mutant gene containing only the native intradiscal cysteine codons.Semantic proximity Read ↗

Conformational insights into the C-terminal mutations of human rhodopsin in retinitispigmentosa.Semantic proximity Read ↗

The effect of triple glutamic mutations E9Q/E194Q/E204Q on the structural stability of bacteriorhodopsin.Semantic proximity Read ↗

G‐protein‐coupled receptor structures were not built in a daySemantic proximity Read ↗

Photoactivation-induced instability of rhodopsin mutants T4K and T17M in rod outer segments underlies retinal degeneration in X. laevis transgenic models of retinitis pigmentosa.Semantic proximity Read ↗

Structure and function in rhodopsin: Mass spectrometric identification of the abnormal intradiscal disulfide bond in misfolded retinitis pigmentosa mutants.Semantic proximity Read ↗

Precision vs flexibility in GPCR signaling.Semantic proximity Read ↗

Structural insights into the mechanism of rhodopsin phosphodiesterase.Semantic proximity Read ↗

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