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 basis for translational inhibition by the tumour suppressor Pdcd4.

The EMBO journal - 4 Feb 2009

Loh Portia G, Yang Hsin-Sheng, Walsh Martin A, Wang Qing, Wang Xiaoxing, Cheng Zhihong, Liu Dingxiang, Song Haiwei

Abstract excerpt

Pdcd4 is a tumour suppressor protein. It inhibits translation through interaction with translation initiator eIF4A, resulting in the suppression of neoplastic transformation and tumour invasion. Here, we present the crystal structures of an N-terminal-truncated Pdcd4 in free form and in complex with eIF4A. Upon binding to eIF4A, Pdcd4 undergoes a marked conformational change to form a heterotrimeric complex with...

Read the complete abstract on PubMed

Topics

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

Share to Apoptosis Regulatory Proteins
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA Helicases

Share to Eukaryotic Initiation Factor-4G

Share to Protein Biosynthesis

Share to RNA-Binding Proteins

Share to Solutions

Share to Transcription Factor AP-1

Source

Open in PubMed Open full text

Identifiers

PMID: 19153607
DOI: 10.1038/emboj.2008.278
PMCID: PMC2637334

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural basis for translational inhibition by the tumour suppressor Pdcd4.PMID 19153607Read ↗

Crystal structure of the eIF4A-PDCD4 complex.Semantic proximity Read ↗

The transformation suppressor Pdcd4 is a novel eukaryotic translation initiation factor 4A binding protein that inhibits translation.Semantic proximity Read ↗

Human tumor suppressor protein Pdcd4 binds at the mRNA entry channel in 40S small ribosomal subunitSemantic proximity Read ↗

The Structures of eIF4E-eIF4G Complexes Reveal an Extended Interface to Regulate Translation Initiation.Semantic proximity Read ↗

An evolutionarily conserved interaction of tumor suppressor protein Pdcd4 with the poly(A)-binding protein contributes to translation suppression by Pdcd4.Semantic proximity Read ↗

Loss-of-function cancer-associated mutations in the EIF4G2 non-canonical translation initiation factorSemantic proximity Read ↗

Loss-of-function cancer-linked mutations in the EIF4G2 non-canonical translation initiation factor.Semantic proximity Read ↗

Targeting the eIF4F translation initiation complex for cancer therapySemantic proximity Read ↗

Structural and Functional Insights into Human Re-initiation Complexes.Semantic proximity Read ↗

Cap-free structure of eIF4E suggests a basis for conformational regulation by its ligands.Semantic proximity Read ↗

Structure of eIF4E in Complex with an eIF4G Peptide Supports a Universal Bipartite Binding Mode for Protein Translation.Semantic proximity Read ↗

Mextli proteins use both canonical bipartite and novel tripartite binding modes to form eIF4E complexes that display differential sensitivity to 4E-BP regulation.Semantic proximity Read ↗

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