ArticleProceedings of the National Academy of Sciences of the United States of America1999
Conformational changes in tertiary structure near the ligand binding site of an integrin I domain.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed.
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- Carbohydrate ligand engagement with CD11b enhances differentiation of tumor-associated myeloid cells for immunotherapy of solid cancers.Journal for immunotherapy of cancer · 2023Article
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- Autotransporter-Mediated Display of Complement Receptor Ligands by Gram-Negative Bacteria Increases Antibody Responses and Limits Disease Severity.Pathogens (Basel, Switzerland) · 2020Article
- The Extracellular, Cellular, and Nuclear Stiffness, a Trinity in the Cancer Resistome-A Review.Frontiers in oncology · 2019Review
- Hemodialysis-related changes in phenotypical features of monocytes.Scientific reports · 2018Article
- Volatile Anesthetic Isoflurane Attenuates Liver Injury in Experimental Polymicrobial Sepsis Model.Translational perioperative and pain medicine · 2018Article
- Differential effects of volatile anesthetics on leukocyte integrin macrophage-1 antigen.Journal of immunotoxicology · 2016Article
- Ligand recognition specificity of leukocyte integrin αMβ2 (Mac-1, CD11b/CD18) and its functional consequences.Biochemistry · 2015Article
- Combined protein- and nucleic acid-level effects of rs1143679 (R77H), a lupus-predisposing variant within ITGAM.Human molecular genetics · 2014Article
- Activation states of blood eosinophils in asthma.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2014Review
- Real-time imaging of Toxoplasma-infected human monocytes under fluidic shear stress reveals rapid translocation of intracellular parasites across endothelial barriers.Cellular microbiology · 2014Article
- Multiple lupus-associated ITGAM variants alter Mac-1 functions on neutrophils.Arthritis and rheumatism · 2013Article
- Tyrosine phosphorylation of CD13 regulates inflammatory cell-cell adhesion and monocyte trafficking.Journal of immunology (Baltimore, Md. : 1950) · 2013Article
- Anti-IL-5 attenuates activation and surface density of β(2) -integrins on circulating eosinophils after segmental antigen challenge.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2013Article
- Integrin activation States and eosinophil recruitment in asthma.Frontiers in pharmacology · 2013Article
- A single disulfide bond disruption in the β3 integrin subunit promotes thiol/disulfide exchange, a molecular dynamics study.PloS one · 2013Article
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3 authors.
Funding
Abstract
For efficient ligand binding, integrins must be activated. Specifically, a conformational change has been proposed in a ligand binding domain present within some integrins, the inserted (I) domain [Lee, J., Bankston, L., Arnaout, M. & Liddington, R. C. (1995) Structure (London) 3, 1333-1340]. This proposal remains controversial, however, despite extensive crystal structure studies on the I domain [Lee, J., Bankston, L., Arnaout, M. & Liddington, R. C. (1995) Structure (London) 3, 1333-1340; Liddington, R. & Bankston, L. (1998) Structure (London) 6, 937-938; Qu, A. & Leahy, D. J. (1996) Structure (London) 4, 931-942; and Baldwin, E. T., Sarver, R. W., Bryant, G. L., Jr., Curry, K. A., Fairbanks, M. B., Finzel, B. C. , Garlick, R. L., Heinrikson, R. L., Horton, N. C. & Kelly, L. L. (1998) Structure (London) 6, 923-935]. By defining the residues present in the epitope of a mAb against the human Mac-1 integrin (alphaMbeta2, CD11b/CD18) that binds only the active receptor, we provide biochemical evidence that the I domain itself undergoes a conformational change with activation. This mAb, CBRM1/5, binds the I domain very close to the ligand binding site in a region that is widely exposed regardless of activation as judged by reactivity with other antibodies. The conformation of the epitope differs in two crystal forms of the I domain, previously suggested to represent active and inactive receptor. Our data suggests that conformational differences in the I domain are physiologically relevant and not merely a consequence of different crystal lattice interactions. We also demonstrate that the transition between the two conformational states depends on species-specific residues at the bottom of the I domain, which are proposed to be in an interface with another integrin domain, and that this transition correlates with functional activity.
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