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Article

The α4β1/EMILIN1 interaction discloses a novel and unique integrin-ligand type of engagement.

Matrix biology : journal of the International Society for Matrix Biology - 1 Mar 2018

Capuano Alessandra, Fogolari Federico, Bucciotti Francesco, Spessotto Paola, Nicolosi Pier Andrea, Mucignat Maria Teresa, Cervi Marta, Esposito Gennaro, Colombatti Alfonso, Doliana Roberto

Abstract excerpt

EMILIN1, a homo-trimeric adhesive ECM glycoprotein, interacts with the α4β1 integrin through its gC1q domain. Uniquely among the C1q family members, the EMILIN1 gC1q presents only nine-stranded β-sandwich fold and the missing strand is substituted by a disordered 19-residue long segment spanning from Y927 to G945 at the apex of the gC1q domain. This unstructured loop exposes to the solvent the acidic residue...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 29037761
DOI: 10.1016/j.matbio.2017.10.001

Genes

EMILIN1

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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