ArticleProceedings of the National Academy of Sciences of the United States of America1993
The CD58 (LFA-3) binding site is a localized and highly charged surface area on the AGFCC'C" face of the human CD2 adhesion domain.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 86 citations in OpenAlex.
- The Structural Biology of T-Cell Antigen Detection at Close Contacts.Immunological reviews · 2025Review
- The m6A revolution: transforming tumor immunity and enhancing immunotherapy outcomes.Cell & bioscience · 2025Review
- HSPA4 upregulation induces immune evasion via ALKBH5/CD58 axis in gastric cancer.Journal of experimental & clinical cancer research : CR · 2024Article
- Structure-based identification of inhibitors disrupting the CD2-CD58 interactions.Journal of computer-aided molecular design · 2021Article
- Multimodal pooled Perturb-CITE-seq screens in patient models define mechanisms of cancer immune evasion.Nature genetics · 2021Article
- CD58 Immunobiology at a Glance.Frontiers in immunology · 2021Review
- Characterizing Post-Translational Modifications and Their Effects on Protein Conformation Using NMR Spectroscopy.Biochemistry · 2020Review
- Costimulatory Function of Cd58/Cd2 Interaction in Adaptive Humoral Immunity in a Zebrafish Model.Frontiers in immunology · 2018Article
- Targeting CD83 for the treatment of graft-versus-host disease.Experimental and therapeutic medicine · 2013Article
- Article
- The core trisaccharide of an N-linked glycoprotein intrinsically accelerates folding and enhances stability.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- A simple detection method for low-affinity membrane protein interactions by baculoviral display.PloS one · 2008Article
- The contribution of conformational adjustments and long-range electrostatic forces to the CD2/CD58 interaction.The Journal of biological chemistry · 2007Article
- Lamina propria T cell activation: role of the costimulatory molecule CD2 and its cytoplasmic tail for the regulation of proliferation and apoptosis.International journal of colorectal disease · 2006Article
- Forced detachment of the CD2-CD58 complex.Biophysical journal · 2003Article
- A feline CD2 homologue interacts with human red blood cells.Immunology · 2002Article
- A space-time structure determination of human CD2 reveals the CD58-binding mode.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Functional glycan-free adhesion domain of human cell surface receptor CD58: design, production and NMR studies.The EMBO journal · 1999Article
- A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion.The EMBO journal · 1998Article
- Visualization of CD2 interaction with LFA-3 and determination of the two-dimensional dissociation constant for adhesion receptors in a contact area.The Journal of cell biology · 1996Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Using site-directed mutagenesis in conjunction with NMR structural data on the adhesion domain of human CD2, we have defined the binding region for CD58. Previous structural studies of rat and human CD2 indicate that this adhesion domain is immunoglobulin-like. Here we report that the CD58 binding site is a well-circumscribed, charged surface area covering approximately 770 A2 on the AGFCC'C" face of the CD2 beta barrel. This site contains beta-strand residues in the carboxyl-terminal half of the F strand (including Lys-82 and Tyr-86), the top of the C strand (Asp-32 and Lys-34), and the C' strand (Gln-46), which are all solvent exposed. In addition, several exposed residues on the FG loop (Gly-90, Lys-91, Asn-92, and Val-93), the CC' loop (Lys-41 and Lys-43), and the C'C" loop (Arg-48 and Lys-51) form this site. In contrast, neither residues on the more peripheral G and C" strands of the same CD2 surface nor residues on B, E, and D strands of the opposite face are involved in CD58 binding. This CD58 binding site is predicted to lie most distal to the T-lymphocyte surface membrane, with ready access to CD58 on the surface of the opposing antigen-presenting cell.
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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.