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

Effects of conformational activation of integrin alpha 1I and alpha 2I domains on selective recognition of laminin and collagen subtypes.

Experimental cell research - 1 May 2008

Tulla Mira, Lahti Matti, Puranen J Santeri, Brandt Anna-Maria, Käpylä Jarmo, Domogatskaya Anna, Salminen Tiina A, Tryggvason Karl, Johnson Mark S, Heino Jyrki

Abstract excerpt

Collagen receptor integrins alpha 1 beta 1 and alpha 2 beta 1 can selectively recognize different collagen subtypes. Here we show that their alpha I domains can discriminate between laminin isoforms as well: alpha 1I and alpha 2I recognized laminin-111, -211 and -511, whereas their binding to laminin-411 was negligible. Residue Arg-218 in alpha1 was found to be instrumental in high-avidity binding. The...

Read the complete abstract on PubMed

Topics

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

Share to Arginine
Share to Collagen

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Integrin alpha2

Share to Laminin

Share to Models, Molecular

Share to Protein Binding

Share to Protein Isoforms

Share to Protein Structure, Tertiary

Source

Identifiers

PMID: 18377895
DOI: 10.1016/j.yexcr.2008.01.025

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

Effects of conformational activation of integrin alpha 1I and alpha 2I domains on selective recognition of laminin and collagen subtypes.PMID 18377895Read ↗

Distinct Recognition of Collagen Subtypes by α1β1 and α2β1IntegrinsSemantic proximity Read ↗

Characterization of alphaX I-domain binding to Thy-1.Semantic proximity Read ↗

Identification of a regulatory region of integrin beta 1 subunit using activating and inhibiting antibodiesSemantic proximity Read ↗

A novel gain-of-function mutation of the integrin alpha2 VWFA domain.Semantic proximity Read ↗

Direct binding of collagen to the I domain of integrin alpha 2 beta 1 (VLA-2, CD49b/CD29) in a divalent cation-independent manner.Semantic proximity Read ↗

Two synergistic activation mechanisms of alpha2beta1 integrin-mediated collagen binding.Semantic proximity Read ↗

Transition from rolling to firm adhesion can be mimicked by extension of integrin alphaLbeta2 in an intermediate affinity state.Semantic proximity Read ↗

Amino acid changes in Drosophila alphaPS2betaPS integrins that affect ligand affinity.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 ↗

Structural and Functional Studies with Antibodies to the Integrin β2 SubunitSemantic proximity Read ↗

An activating mutation reveals a second binding mode of the integrin α2 I domain to the GFOGER motif in collagens.Semantic proximity Read ↗

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

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