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

Mapping of contact sites in complex formation between light-activated rhodopsin and transducin by covalent crosslinking: use of a chemically preactivated reagent.

Proceedings of the National Academy of Sciences of the United States of America - 24 Apr 2001

Itoh Y, Cai K, Khorana H G

Abstract excerpt

Contact sites in interaction between light-activated rhodopsin and transducin (T) have been investigated by using a chemically preactivated crosslinking reagent, N-succinimidyl 3-(2-pyridyldithio)propionate. The 3 propionyl-N-succinimidyl group in the reagent was attached by a disulfide exchange reaction to rhodopsin mutants containing single reactive cysteine groups in the cytoplasmic loops. Complex formation...

Read the complete abstract on PubMed

Topics

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

Share to Azides
Share to Cross-Linking Reagents

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Subunits

Share to Pyridines

Share to Rhodopsin

Share to Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Share to Succinimides

Share to Transducin

Source

Open in PubMed Open full text

Identifiers

PMID: 11320238
DOI: 10.1073/pnas.051632998
PMCID: PMC33132

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mapping of contact sites in complex formation between light-activated rhodopsin and transducin by covalent crosslinking: use of a chemically preactivated reagent.PMID 11320238Read ↗

Mapping of contact sites in complex formation between transducin and light-activated rhodopsin by covalent crosslinking: use of a photoactivatable reagent.Semantic proximity Read ↗

Rhodopsin determinants for transducin activation: a gain-of-function approach.Semantic proximity Read ↗

Rhodopsin activation exposes a key hydrophobic binding site for the transducin alpha-subunit C terminus.Semantic proximity Read ↗

Rhodopsin-transducin interface: studies with conformationally constrained peptides.Semantic proximity Read ↗

Intramolecular interactions that induce helical rearrangement upon rhodopsin activation: light-induced structural changes in metarhodopsin IIa probed by cysteine S-H stretching vibrations.Semantic proximity Read ↗

The cytoplasmic membrane-proximal domain of the HtrII transducer interacts with the E-F loop of photoactivated Natronomonas pharaonis sensory rhodopsin II.Semantic proximity Read ↗

Tyr-199 and charged residues of pharaonis Phoborhodopsin are important for the interaction with its transducer.Semantic proximity Read ↗

Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin.Semantic proximity Read ↗

Conformations of the rhodopsin third cytoplasmic loop grafted onto bacteriorhodopsin.Semantic proximity Read ↗

Regioselective Chemical Modification of Cysteine Residues on Protein Surfaces Focusing on Local Environment around the Conjugation Site.Semantic proximity Read ↗

Association between a photo-intermediate of a M-lacking mutant D75N of pharaonis phoborhodopsin and its cognate transducer.Semantic proximity Read ↗

Photocrosslinking of benzophenone-labeled single cysteine troponin I mutants to other thin filament proteins.Semantic proximity Read ↗

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