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

Solution NMR structure of the SH3 domain of human nephrocystin and analysis of a mutation-causing juvenile nephronophthisis.

Proteins - 1 May 2005

le Maire Albane, Weber Thomas, Saunier Sophie, Broutin Isabelle, Antignac Corinne, Ducruix Arnaud, Dardel Frédéric

Abstract excerpt

Human nephrocystin is a protein associated with juvenile NPH, an autosomal recessive, inherited kidney disease responsible for chronic renal failure in children. It contains an SH3 domain involved in signaling pathways controlling cell adhesion and cytoskeleton organization. The solution structure of this domain was solved by triple resonance NMR spectroscopy. Within the core, the structure is similar to those...

Read the complete abstract on PubMed

Topics

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

Share to Adaptor Proteins, Signal Transducing
Share to Cytoskeletal Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Kidney Diseases, Cystic

Share to Magnetic Resonance Spectroscopy

Share to Models, Molecular

Share to Protein Conformation

Share to Proteins

Share to src Homology Domains

Source

Identifiers

PMID: 15723349
DOI: 10.1002/prot.20344

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

Solution NMR structure of the SH3 domain of human nephrocystin and analysis of a mutation-causing juvenile nephronophthisis.PMID 15723349Read ↗

Nephrocystin-conserved Domains Involved in Targeting to Epithelial Cell-Cell Junctions, Interaction with Filamins, and Establishing Cell PolaritySemantic proximity Read ↗

The gene mutated in juvenile nephronophthisis type 4 encodes a novel protein that interacts with nephrocystin.Semantic proximity Read ↗

A novel gene encoding an SH3 domain protein is mutated in nephronophthisis type 1.Semantic proximity Read ↗

Structure and interactions of the CS domain of human H/ACA RNP assembly protein Shq1.Semantic proximity Read ↗

The redundancy of NMR restraints can be used to accelerate the unfolding behavior of an SH3 domain during molecular dynamics simulations.Semantic proximity Read ↗

Investigation of binding phenomenon of NSP3 and p130Cas mutants and their effect on cell signalling.Semantic proximity Read ↗

β1 integrin NPXY motifs regulate kidney collecting-duct development and maintenance by induced-fit interactions with cytosolic proteins.Semantic proximity Read ↗

¹H, ¹³C, and ¹⁵N assignments of wild-type human γS-crystallin and its cataract-related variant γS-G18V.Semantic proximity Read ↗

Flexible Structures of SIBLING Proteins, Bone Sialoprotein, and OsteopontinSemantic proximity Read ↗

Solution NMR structures of IgG binding domains with artificially evolved high levels of sequence identity but different folds.Semantic proximity Read ↗

Effect of N-terminal and Met23 mutations on the structure and dynamics of onconase.Semantic proximity Read ↗

Structural and biophysical insights into the ligand-free Pitx2 homeodomain and a ring dermoid of the cornea inducing homeodomain mutant.Semantic proximity Read ↗

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