ArticleProceedings of the National Academy of Sciences of the United States of America2016
Leukocyte integrin αLβ2 headpiece structures: The αI domain, the pocket for the internal ligand, and concerted movements of its loops.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 32 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
32 citing papers in PubMed.
- Integrin-mediated mechanotransduction in the tumor microenvironment: macrophage-centered signaling mechanisms and immune remodeling.Journal of translational medicine · 2026Review
- Functional unfolding of the integrin αX transmembrane helix.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Molecular exaptation by the integrin αI domain.Science advances · 2025Article
- ISG-15, beyond its functions in the cell: a mini review.Cellular and molecular life sciences : CMLS · 2025Review
- NPC1L1 on pancreatic adenocarcinoma cell functions as a two-pronged checkpoint against antitumor activity.Innovation (Cambridge (Mass.)) · 2025Article
- Screening of Phytocompounds Against the NF-kB Pathway Genes and Lung Elevated Proteins Associated with Acute Respiratory Distress Syndrome.Recent advances in inflammation & allergy drug discovery · 2025Article
- Review
- Structural surfaceomics reveals an AML-specific conformation of integrin βNature cancer · 2023Article
- Family-wide analysis of integrin structures predicted by AlphaFold2.bioRxiv : the preprint server for biology · 2023Article
- Systematic mapping of the conformational landscape and dynamism of soluble fibrinogen.Journal of thrombosis and haemostasis : JTH · 2023Article
- Antigen discrimination by T cells relies on size-constrained microvillar contact.Nature communications · 2023Article
- Structural biology of complement receptors.Frontiers in immunology · 2023Review
- Family-wide analysis of integrin structures predicted by AlphaFold2.Computational and structural biotechnology journal · 2023Article
- Heterotropic roles of divalent cations in the establishment of allostery and affinity maturation of integrin αXβ2.Cell reports · 2022Article
- CD11b agonists offer a novel approach for treating lupus nephritis.Translational research : the journal of laboratory and clinical medicine · 2022Review
- Machine learning/molecular dynamic protein structure prediction approach to investigate the protein conformational ensemble.Scientific reports · 2022Article
- The crystal structure of iC3b-CR3 αI reveals a modular recognition of the main opsonin iC3b by the CR3 integrin receptor.Nature communications · 2022Article
- Natural Killer Cell Integrins and Their Functions in Tissue Residency.Frontiers in immunology · 2021Review
- Mechanically Regulated Outside-In Activation of an I-Domain-Containing Integrin.Biophysical journal · 2020Article
- Molecular mechanism of leukocidin GH-integrin CD11b/CD18 recognition and species specificity.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
Corrections and comments
- Erratum issued
Authors and funding
2 authors.
Funding
Abstract
High-resolution crystal structures of the headpiece of lymphocyte function-associated antigen-1 (integrin αLβ2) reveal how the αI domain interacts with its platform formed by the α-subunit β-propeller and β-subunit βI domains. The αLβ2 structures compared with αXβ2 structures show that the αI domain, tethered through its N-linker and a disulfide to a stable β-ribbon pillar near the center of the platform, can undergo remarkable pivoting and tilting motions that appear buffered by N-glycan decorations that differ between αL and αX subunits. Rerefined β2 integrin structures reveal details including pyroglutamic acid at the β2 N terminus and bending within the EGF1 domain. Allostery is relayed to the αI domain by an internal ligand that binds to a pocket at the interface between the β-propeller and βI domains. Marked differences between the αL and αX subunit β-propeller domains concentrate near the binding pocket and αI domain interfaces. Remarkably, movement in allostery in the βI domain of specificity determining loop 1 (SDL1) causes concerted movement of SDL2 and thereby tightens the binding pocket for the internal ligand.
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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.