ArticleThe EMBO journal1999
Functional glycan-free adhesion domain of human cell surface receptor CD58: design, production and NMR studies.
Article in The EMBO journal, 1999. 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, 40 citations in OpenAlex.
- Structure-based identification of inhibitors disrupting the CD2-CD58 interactions.Journal of computer-aided molecular design · 2021Article
- CD58 Immunobiology at a Glance.Frontiers in immunology · 2021Review
- Costimulatory Function of Cd58/Cd2 Interaction in Adaptive Humoral Immunity in a Zebrafish Model.Frontiers in immunology · 2018Article
- Scoring function to predict solubility mutagenesis.Algorithms for molecular biology : AMB · 2010Article
- Overcoming the solubility limit with solubility-enhancement tags: successful applications in biomolecular NMR studies.Journal of biomolecular NMR · 2010Article
- The contribution of conformational adjustments and long-range electrostatic forces to the CD2/CD58 interaction.The Journal of biological chemistry · 2007Article
- Identification of individual protein-ligand NOEs in the limit of intermediate exchange.Journal of biomolecular NMR · 2006Article
- Structure-activity studies of peptides from the "hot-spot" region of human CD2 protein: development of peptides for immunomodulation.Journal of medicinal chemistry · 2005Article
- Using codon optimization, chaperone co-expression, and rational mutagenesis for production and NMR assignments of human eIF2 alpha.Journal of biomolecular NMR · 2004Article
- Documentation of immune profile of microglia through cell surface marker study in glioma model primed by a novel cell surface glycopeptide T11TS/SLFA-3.Glycoconjugate journal · 2004Article
- Specificity and affinity of sialic acid binding by the rhesus rotavirus VP8* core.Journal of virology · 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
- Solution structure of Apaf-1 CARD and its interaction with caspase-9 CARD: a structural basis for specific adaptor/caspase interaction.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
A general strategy is presented here for producing glycan-free forms of glycoproteins without loss of function by employing apolar-to-polar mutations of surface residues in functionally irrelevant epitopes. The success of this structure-based approach was demonstrated through the expression in Escherichia coli of a soluble 11 kDa adhesion domain extracted from the heavily glycosylated 55 kDa human CD58 ectodomain. The solution structure was subsequently determined and binding to its counter-receptor CD2 studied by NMR. This mutant adhesion domain is functional as determined by several experimental methods, and the size of its binding site has been probed by chemical shift perturbations in NMR titration experiments. The new structural information supports a 'hand-shake' model of CD2-CD58 interaction involving the GFCC'C" faces of both CD2 and CD58 adhesion domains. The region responsible for binding specificity is most likely localized on the C, C' and C" strands and the C-C' and C'-C" loops on CD58.
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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.