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 studies of KCTD1 and its disease-causing mutant P20S provide insights into the protein function and misfunction.

International journal of biological macromolecules - 1 Oct 2024

Balasco Nicole, Ruggiero Alessia, Smaldone Giovanni, Pecoraro Giovanni, Coppola Luigi, Pirone Luciano, Pedone Emilia M, Esposito Luciana, Berisio Rita, Vitagliano Luigi

Abstract excerpt

Members of the KCTD protein family play key roles in fundamental physio-pathological processes including cancer, neurodevelopmental/neuropsychiatric, and genetic diseases. Here, we report the crystal structure of the KCTD1 P20S mutant, which causes the scalp-ear-nipple syndrome, and molecular dynamics (MD) data on the wild-type protein. Surprisingly, the structure unravels that the N-terminal region, which...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Co-Repressor Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Molecular Dynamics Simulation

Share to Mutation

Share to Protein Domains

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 39111466
DOI: 10.1016/j.ijbiomac.2024.134390

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural studies of KCTD1 and its disease-causing mutant P20S provide insights into the protein function and misfunction.PMID 39111466Read ↗

Structural studies of KCTD1 and its disease-causing mutant P20S provide insights into the protein function and misfunctionSemantic proximity Read ↗

A BTB extension and ion-binding domain contribute to the pentameric structure and TFAP2A binding of KCTD1.Semantic proximity Read ↗

A BTB extension and ion-binding domain contribute to the pentameric structure and TFAP2A binding of KCTD1Semantic proximity Read ↗

KCTD10 p.C124W variant contributes to schizophrenia by attenuating LLPS-mediated synapse formation.Semantic proximity Read ↗

Structural model of the TRPP2/PKD1 C-terminal coiled-coil complex produced by a combined computational and experimental approach.Semantic proximity Read ↗

KCTD1 mutants in scalp‑ear‑nipple syndrome and AP‑2α P59A in Char syndrome reciprocally abrogate their interactions, but can regulate Wnt/β‑catenin signaling.Semantic proximity Read ↗

The C66W mutation in the deafness dystonia peptide 1 (DDP1) affects the formation of functional DDP1.TIM13 complexes in the mitochondrial intermembrane space.Semantic proximity Read ↗

Crystal structures of a ZIP zinc transporter reveal a binuclear metal center in the transport pathway.Semantic proximity Read ↗

Deciphering ion transport and ATPase coupling in the intersubunit tunnel of KdpFABC.Semantic proximity Read ↗

The C-terminal cytosolic domain of the human zinc transporter ZnT8 and its diabetes risk variant.Semantic proximity Read ↗

Structural insights into lethal contractural syndrome type 3 (LCCS3) caused by a missense mutation of PIP5Kγ.Semantic proximity Read ↗

Integrating biological regulatory network analysis and structural bioinformatics to probe CABP4 transcriptional regulation in night blindness.Semantic proximity Read ↗

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