ArticlePloS one2013
An activating mutation reveals a second binding mode of the integrin α2 I domain to the GFOGER motif in collagens.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 37 citations in OpenAlex.
- Nanoscale Structural and Functional Impacts of Disease-Associated Collagen Mutations.bioRxiv : the preprint server for biology · 2025Article
- Interactions of Cardiac Proteins with Plasma-Synthesized Polypyrrole (PSPy) to Improve Adult Cardiomyocytes Culture.Polymers · 2024Article
- Designing collagens to shed light on the multi-scale structure-function mapping of matrix disorders.Matrix biology plus · 2024Review
- Organoid co-culture model of the human endometrium in a fully synthetic extracellular matrix enables the study of epithelial-stromal crosstalk.Med (New York, N.Y.) · 2023Article
- Collagen's primary structure determines collagen:HSP47 complex stoichiometry.The Journal of biological chemistry · 2021Article
- Selectivity of the collagen-binding integrin inhibitors, TC-I-15 and obtustatin.Toxicology and applied pharmacology · 2021Article
- Structural and biophysical characterization of the type VII collagen vWFA2 subdomain leads to identification of two binding sites.FEBS open bio · 2020Article
- Reciprocal Interplay Between Fibrillar Collagens and Collagen-Binding Integrins: Implications in Cancer Progression and Metastasis.Frontiers in oncology · 2020Review
- COMP and TSP-4 interact specifically with the novel GXKGHR motif only found in fibrillar collagens.Scientific reports · 2018Article
- Roles of PLODs in Collagen Synthesis and Cancer Progression.Frontiers in cell and developmental biology · 2018Review
- Revealing Accessibility of Cryptic Protein Binding Sites within the Functional Collagen Fibril.Biomolecules · 2017Review
- Parallels between DNA and collagen - comparing elastic models of the double and triple helix.Scientific reports · 2017Article
- Structural insight for chain selection and stagger control in collagen.Scientific reports · 2016Article
- Mapping the Effect of Gly Mutations in Collagen on α2β1 Integrin Binding.The Journal of biological chemistry · 2016Article
- Intrinsic local destabilization of the C-terminus predisposes integrin α1 I domain to a conformational switch induced by collagen binding.Protein science : a publication of the Protein Society · 2016Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The GFOGER motif in collagens (O denotes hydroxyproline) represents a high-affinity binding site for all collagen-binding integrins. Other GxOGER motifs require integrin activation for maximal binding. The E318W mutant of the integrin α2β1 I domain displays a relaxed collagen specificity, typical of an active state. E318W binds more strongly than the wild-type α2 I domain to GMOGER, and forms a 2:1 complex with a homotrimeric, collagen-like, GFOGER peptide. Crystal structure analysis of this complex reveals two E318W I domains, A and B, bound to a single triple helix. The E318W I domains are virtually identical to the collagen-bound wild-type I domain, suggesting that the E318W mutation activates the I domain by destabilising the unligated conformation. E318W I domain A interacts with two collagen chains similarly to wild-type I domain (high-affinity mode). E318W I domain B makes favourable interactions with only one collagen chain (low-affinity mode). This observation suggests that single GxOGER motifs in the heterotrimeric collagens V and IX may support binding of activated integrins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.