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

Magnesium Activates Microsecond Dynamics to Regulate Integrin-Collagen Recognition.

Structure (London, England : 1993) - 7 Aug 2018

Nunes Ana Monica, Minetti Conceição A S A, Remeta David P, Baum Jean

Abstract excerpt

Integrin receptors bind collagen via metal-mediated interactions that are modulated by magnesium (Mg2+) levels in the extracellular matrix. Nuclear magnetic resonance-based relaxation experiments, isothermal titration calorimetry, and adhesion assays reveal that Mg2+ functions as both a structural anchor and dynamic switch of the α1β1 integrin I domain (α1I). Specifically, Mg2+ binding activates micro- to...

Read the complete abstract on PubMed

Topics

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

Share to Cations, Divalent
Share to Collagen Type I
Share to Extracellular Matrix

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Magnesium

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Protein Conformation, alpha-Helical

Share to Protein Conformation, beta-Strand

Share to Protein Interaction Domains and Motifs

Source

Open in PubMed Open full text

Identifiers

PMID: 29937357
DOI: 10.1016/j.str.2018.05.010
PMCID: PMC6615728

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Magnesium Activates Microsecond Dynamics to Regulate Integrin-Collagen Recognition.PMID 29937357Read ↗

Structures of the alpha L I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation.Semantic proximity Read ↗

A pivotal role for a conserved bulky residue at the α1-helix of the αI integrin domain in ligand binding.Semantic proximity Read ↗

Integrin activation involves a conformational change in the alpha 1 helix of the beta subunit A-domain.Semantic proximity Read ↗

ATP allosterically stabilizes Integrin-linked kinase for efficient force generationSemantic proximity Read ↗

Structural basis for regulation of human calcium-sensing receptor by magnesium ions and an unexpected tryptophan derivative co-agonist.Semantic proximity Read ↗

Structure of collagen receptor integrin α(1)I domain carrying the activating mutation E317A.Semantic proximity Read ↗

Variation in one residue associated with the metal ion-dependent adhesion site regulates αIIbβ3 integrin ligand binding affinity.Semantic proximity Read ↗

Molecular tuning of an EF-hand-like calcium binding loop. Contributions of the coordinating side chain at loop position 3.Semantic proximity Read ↗

Structural determinants of calcium binding beyond the EF-hand binding site: a study of alpha parvalbuminsSemantic proximity Read ↗

The relative influence of metal ion binding sites in the I-like domain and the interface with the hybrid domain on rolling and firm adhesion by integrin alpha4beta7.Semantic proximity Read ↗

Impact of salt concentration and free magnesium on human beta-cardiac myosin reveal important details about the conserved mechanochemical mechanism.Semantic proximity Read ↗

Functional and computational studies of the ligand-associated metal binding site of beta3 integrins.Semantic proximity Read ↗

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