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

Snapshot of protein structure evolution reveals conservation of functional dimerization through intertwined folding.

Structure (London, England : 1993) - 1 Aug 2004

Chirgadze Dimitri Y, Demydchuk Mykhaylo, Becker Marion, Moran Stephen, Paoli Massimo

Abstract excerpt

Protein-protein interactions govern a wide range of cellular processes. Molecular recognition responsible for homodimerization and heterodimerization in the rel/NF-kappaB family of eukaryotic transcription factors relies on a small cluster of hydrophobic residues. We have carried out a structural analysis of six NF-kappaB p50 dimer interface mutants; one of them revealed a remarkable alteration. One or possibly...

Read the complete abstract on PubMed

Topics

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

Share to Crystallography, X-Ray
Share to Dimerization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Evolution, Molecular

Share to Hydrophobic and Hydrophilic Interactions

Share to Models, Molecular

Share to Protein Binding

Share to Protein Folding

Share to Protein Serine-Threonine Kinases

Source

Identifiers

PMID: 15296742
DOI: 10.1016/j.str.2004.06.011

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

Snapshot of protein structure evolution reveals conservation of functional dimerization through intertwined folding.PMID 15296742Read ↗

Mutational analysis of the kinetics and thermodynamics of transcription factor NF-kappaB homodimerisation.Semantic proximity Read ↗

An overview of the processes shaping protein evolution.Semantic proximity Read ↗

Molecular dimension explored in evolution to promote proteomic complexity.Semantic proximity Read ↗

Evolution of oligomeric state through allosteric pathways that mimic ligand binding.Semantic proximity Read ↗

Sequence-structure signals of 3D domain swapping in proteins.Semantic proximity Read ↗

The design and characterization of two proteins with 88% sequence identity but different structure and function.Semantic proximity Read ↗

A structural view of evolutionary divergence.Semantic proximity Read ↗

Structure, function, and evolution of transient and obligate protein-protein interactions.Semantic proximity Read ↗

Structural basis of affinity maturation and intramolecular cooperativity in a protein-protein interaction.Semantic proximity Read ↗

Allosteric and energetic remodeling of a PDZ domain by protein domain extensions.Semantic proximity Read ↗

Predicting the Effect of Mutations on Protein-Protein Binding Interactions through Structure-Based Interface Profiles.Semantic proximity Read ↗

Domain-Swapped Dimers of Intracellular Lipid-Binding Proteins: Evidence for Ordered Folding Intermediates.Semantic proximity Read ↗

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