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

Characterization of the SRP68/72 interface of human signal recognition particle by systematic site-directed mutagenesis.

Protein science : a publication of the Protein Society - 1 Oct 2009

Iakhiaeva Elena, Hinck Cynthia S, Hinck Andrew P, Zwieb Christian

Abstract excerpt

The signal recognition particle (SRP) is a ribonucleoprotein complex which is crucial for the delivery of proteins to cellular membranes. Among the six proteins of the eukaryotic SRP, the two largest, SRP68 and SRP72, form a stable SRP68/72 heterodimer of unknown structure which is required for SRP function. Fragments 68e' (residues 530 to 620) and 72b' (residues 1 to 166) participate in the SRP68/72 interface....

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Mutagenesis, Site-Directed

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

Share to Mutant Proteins

Share to Mutation

Share to Protein Binding

Share to Signal Recognition Particle

Source

Open in PubMed Open full text

Identifiers

PMID: 19693936
DOI: 10.1002/pro.232
PMCID: PMC2786981

Genes

SRP68
SRP72

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

Characterization of the SRP68/72 interface of human signal recognition particle by systematic site-directed mutagenesis.PMID 19693936Read ↗

Human apo-SRP72 and SRP68/72 complex structures reveal the molecular basis of protein translocation.Semantic proximity Read ↗

Roles for Srp72p in assembly, nuclear export and function of the signal recognition particle.Semantic proximity Read ↗

Binding site of the M-domain of human protein SRP54 determined by systematic site-directed mutagenesis of signal recognition particle RNA.Semantic proximity Read ↗

Solution structure of protein SRP19 of Archaeoglobus fulgidus signal recognition particle.Semantic proximity Read ↗

Molecular evolution of SRP cycle components: functional implications.Semantic proximity Read ↗

Assembly of the human signal recognition particle (SRP): overlap of regions required for binding of protein SRP54 and assembly control.Semantic proximity Read ↗

Site-directed mutagenesis of signal-recognition particle RNA. Identification of the nucleotides in helix 8 required for interaction with protein SRP19.Semantic proximity Read ↗

Two strategically placed base pairs in helix 8 of mammalian signal recognition particle RNA are crucial for the SPR19-dependent binding of protein SRP54.Semantic proximity Read ↗

The signal recognition particle (SRP) RNA links conformational changes in the SRP to protein targeting.Semantic proximity Read ↗

Characterization of human herpesvirus 6A/B U94 as ATPase, helicase, exonuclease and DNA-binding proteinsSemantic proximity Read ↗

Interaction of protein SRP19 with signal recognition particle RNA lacking individual RNA-helices.Semantic proximity Read ↗

Structure of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome.Semantic proximity Read ↗

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