ArticleThe Journal of experimental medicine1994
Interaction between human CD2 and CD58 involves the major beta sheet surface of each of their respective adhesion domains.
Article in The Journal of experimental medicine, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 42 citations in OpenAlex.
- The Structural Biology of T-Cell Antigen Detection at Close Contacts.Immunological reviews · 2025Review
- The CD58-CD2 axis is co-regulated with PD-L1 via CMTM6 and shapes anti-tumor immunity.Cancer cell · 2023Article
- The contribution of conformational adjustments and long-range electrostatic forces to the CD2/CD58 interaction.The Journal of biological chemistry · 2007Article
- Identification and characterization of the rat homologue of LAIR-1.Immunogenetics · 2005Article
- Forced detachment of the CD2-CD58 complex.Biophysical journal · 2003Article
- CD2 molecules redistribute to the uropod during T cell scanning: implications for cellular activation and immune surveillance.Proceedings of the National Academy of Sciences of the United States of America · 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
- Crystal structure of the CD2-binding domain of CD58 (lymphocyte function-associated antigen 3) at 1.8-A resolution.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- CD48-deficient mice have a pronounced defect in CD4(+) T cell activation.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion.The EMBO journal · 1998Article
- The counterreceptor binding site of human CD2 exhibits an extended surface patch with multiple conformations fluctuating with millisecond to microsecond motions.Protein science : a publication of the Protein Society · 1997Article
- Glycosylphosphatidylinositol (GPI)-anchored surface antigens in the allogeneic activation of T cells.Clinical and experimental immunology · 1995Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The CD58 binding site on human CD2 was recently shown by nuclear magnetic resonance structural data in conjunction with site-directed mutagenesis to be a highly charged surface area covering approximately 770A2 on the major AGFCC'C" face of the CD2 immunoglobulin-like (Ig-like) NH2-terminal domain. Here we have identified the other binding surface of the CD2-CD58 adhesion pair by mutating charged residues shared among CD2 ligands (human CD58, sheep CD58, and human CD48) that are predicted to be solvent exposed on a molecular model of the Ig-like adhesion domain of human CD58. This site includes beta strand residues along the C strand (E25, K29, and K30), in the middle of the C' strand (E37) and in the G strand (K87). In addition, several residues on the CC' loop (K32, D33, and K34) form this site. Thus, the interaction between CD2 and CD58 involves the major beta sheet surface of each adhesion domain. Possible docking orientations for the CD2-CD58 molecular complex are offered. Strict conservation of human and sheep CD58 residues within the involved C and C' strands and CC' loop suggests that this region is particularly important for stable formation of the CD2-CD58 complex. The analysis of this complex offers molecular insight into the nature of a receptor-ligand pair involving two Ig family members.
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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.