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

The structure of the scaffold nucleoporin Nup120 reveals a new and unexpected domain architecture.

Structure (London, England : 1993) - 12 Aug 2009

Leksa Nina C, Brohawn Stephen G, Schwartz Thomas U

Abstract excerpt

Nucleocytoplasmic transport is mediated by nuclear pore complexes (NPCs), enormous protein assemblies residing in circular openings in the nuclear envelope. The NPC is modular, with transient and stable components. The stable core is essentially built from two multiprotein complexes, the Y-shaped heptameric Nup84 complex and the Nic96 complex, arranged around an eightfold axis. We present the crystal structure of...

Read the complete abstract on PubMed

Topics

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

Share to Chromatography, Gel
Share to Crystallization
Share to Microscopy, Fluorescence

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Multiprotein Complexes

Share to Nuclear Pore

Share to Nuclear Pore Complex Proteins

Share to Protein Folding

Share to Static Electricity

Source

Open in PubMed Open full text

Identifiers

PMID: 19576787
DOI: 10.1016/j.str.2009.06.003
PMCID: PMC2743489

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

The structure of the scaffold nucleoporin Nup120 reveals a new and unexpected domain architecture.PMID 19576787Read ↗

Structural and functional analysis of Nup120 suggests ring formation of the Nup84 complex.Semantic proximity Read ↗

Molecular basis for Nup37 and ELY5/ELYS recruitment to the nuclear pore complex.Semantic proximity Read ↗

The nuclear pore complex: understanding its function through structural insight.Semantic proximity Read ↗

Architecture of the linker-scaffold in the nuclear poreSemantic proximity Read ↗

Structure and assembly of the Nup84p complex.Semantic proximity Read ↗

Integrative structure-function mapping of the nucleoporin Nup133 suggests a conserved mechanism for membrane anchoring of the nuclear pore complex.Semantic proximity Read ↗

Mutations in nucleoporins and their roles in human diseases: Integrating evidence on specific NUP functions.Semantic proximity Read ↗

Stoichiometry and compositional plasticity of the yeast nuclear pore complex revealed by quantitative fluorescence microscopySemantic proximity Read ↗

Nuclear pore complex composition: a new regulator of tissue-specific and developmental functions.Semantic proximity Read ↗

Advances in the understanding of nuclear pore complexes in human diseasesSemantic proximity Read ↗

The yeast nucleoporin Nup53p specifically interacts with Nic96p and is directly involved in nuclear protein import.Semantic proximity Read ↗

The nuclear pore complex.Semantic proximity Read ↗

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