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

Family-wide Structural and Biophysical Analysis of Binding Interactions among Non-clustered δ-Protocadherins.

Cell reports - 25 Feb 2020

Harrison Oliver J, Brasch Julia, Katsamba Phinikoula S, Ahlsen Goran, Noble Alex J, Dan Hanbin, Sampogna Rosemary V, Potter Clinton S, Carragher Bridget, Honig Barry, Shapiro Lawrence

Abstract excerpt

Non-clustered δ1- and δ2-protocadherins, close relatives of clustered protocadherins, function in cell adhesion and motility and play essential roles in neural patterning. To understand the molecular interactions underlying these functions, we used solution biophysics to characterize binding of δ1- and δ2-protocadherins, determined crystal structures of ectodomain complexes from each family, and assessed...

Read the complete abstract on PubMed

Topics

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

Share to Biophysical Phenomena
Share to Cadherins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Liposomes

Share to Protein Domains

Share to Protein Multimerization

Share to Solutions

Share to Surface Plasmon Resonance

Share to Xenopus

Source

Open in PubMed Open full text

Identifiers

PMID: 32101743
DOI: 10.1016/j.celrep.2020.02.003
PMCID: PMC7082078

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Family-wide Structural and Biophysical Analysis of Binding Interactions among Non-clustered δ-Protocadherins.PMID 32101743Read ↗

Homophilic and Heterophilic Interactions of Type II Cadherins Identify Specificity Groups Underlying Cell-Adhesive Behavior.Semantic proximity Read ↗

Interaction specificity of clustered protocadherins inferred from sequence covariation and structural analysis.Semantic proximity Read ↗

Antiparallel protocadherin homodimers use distinct affinity- and specificity-mediating regions in cadherin repeats 1-4Semantic proximity Read ↗

Microfibril-associated glycoprotein 4 forms octamers that mediate interactions with elastogenic proteins and cellsSemantic proximity Read ↗

The molecular architecture of the desmosomal outer dense plaque by integrative structural modelingSemantic proximity Read ↗

Structure and Function of Hemidesmosomes: More Than Simple Adhesion ComplexesSemantic proximity Read ↗

T-cadherin structures reveal a novel adhesive binding mechanism.Semantic proximity Read ↗

The conformation of tetraspanins CD53 and CD81 differentially affects their nanoscale organization and interaction with their partners.Semantic proximity Read ↗

Microscopic clusters feature the composition of biochemical tetraspanin-assemblies and constitute building-blocks of tetraspanin enriched domainsSemantic proximity Read ↗

Combinatorial homophilic interaction between gamma-protocadherin multimers greatly expands the molecular diversity of cell adhesion.Semantic proximity Read ↗

Cryo-EM reveals a right-handed double-helix dimer architecture of PCDH15.Semantic proximity Read ↗

Lateral assembly of N-cadherin drives tissue integrity by stabilizing adherens junctions.Semantic proximity Read ↗

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