Reversible inactivation of AT(2) angiotensin II receptor from cysteine-disulfide bond exchange.

doi:10.1016/s0014-5793(00)02141-4

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

Back to search

Article

Reversible inactivation of AT(2) angiotensin II receptor from cysteine-disulfide bond exchange.

FEBS letters - 3 Nov 2000

Feng Y H, Saad Y, Karnik S S

Abstract excerpt

Dithiothreitol (DTT) treatment of angiotensin II (Ang II) type 2 (AT(2)) receptor potentiates ligand binding, but the underlying mechanism is not known. Two disulfide bonds proposed in the extracellular domain were examined in this report. Based on the analysis of ligand affinity of cysteine (Cys, C) to alanine (Ala, A) substitution mutants, we provide evidence that Cys(35)-Cys(290) and Cys(117)-Cys(195)...

Topics

Alanine
Amino Acid Sequence
Amino Acid Substitution
Animals
Binding, Competitive
COS Cells
Cysteine
Disulfides
Dithiothreitol
Molecular Sequence Data
Mutation
Protein Conformation
Rats
Rats, Inbred SHR
Receptor, Angiotensin, Type 1
Receptor, Angiotensin, Type 2
Receptors, Angiotensin
Recombinant Proteins

Source

Open in PubMed

Identifiers

PMID: 11068047
DOI: 10.1016/s0014-5793(00)02141-4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics