ArticleProtein science : a publication of the Protein Society1997
The counterreceptor binding site of human CD2 exhibits an extended surface patch with multiple conformations fluctuating with millisecond to microsecond motions.
Article in Protein science : a publication of the Protein Society, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Glycosylation States on Intact Proteins Determined by NMR Spectroscopy.Molecules (Basel, Switzerland) · 2021Article
- Secretion, isotopic labeling and deglycosylation of N-acylethanolamine acid amidase for biophysical studies.Protein expression and purification · 2018Article
- Effective isotope labeling of proteins in a mammalian expression system.Methods in enzymology · 2015Article
- Mammalian production of an isotopically enriched outer domain of the HIV-1 gp120 glycoprotein for NMR spectroscopy.Journal of biomolecular NMR · 2011Article
- Rational design of protein-based MRI contrast agents.Journal of the American Chemical Society · 2008Article
- Isotope labeling of mammalian GPCRs in HEK293 cells and characterization of the C-terminus of bovine rhodopsin by high resolution liquid NMR spectroscopy.Journal of biomolecular NMR · 2008Article
- The contribution of conformational adjustments and long-range electrostatic forces to the CD2/CD58 interaction.The Journal of biological chemistry · 2007Article
- PhosphoThr peptide binding globally rigidifies much of the FHA domain from Arabidopsis receptor kinase-associated protein phosphatase.Biochemistry · 2005Article
- Backbone dynamics of the 8 kDa dynein light chain dimer reveals molecular basis of the protein's functional diversity.Journal of biomolecular NMR · 2002Article
- A dynamically tuned double-stranded RNA binding mechanism for the activation of antiviral kinase PKR.The EMBO journal · 2000Article
- Backbone dynamics measurements on leukemia inhibitory factor, a rigid four-helical bundle cytokine.Protein science : a publication of the Protein Society · 2000Article
- 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
- NMR exchange broadening arising from specific low affinity protein self-association: analysis of nitrogen-15 nuclear relaxation for rat CD2 domain 1.Journal of biomolecular NMR · 1999Article
- 'Wave-type' structure of a synthetic hexaglycosylated decapeptide: a part of the extracellular domain of human glycophorin A.Journal of biomolecular NMR · 1999Article
- Separating the contributions to 15N transverse relaxation in a fibronectin type III domain.Journal of biomolecular NMR · 1999Article
- Production of large quantities of isotopically labeled protein in Pichia pastoris by fermentation.Journal of biomolecular NMR · 1999Article
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3 authors.
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No grant is acknowledged in the PubMed record.
Abstract
We have used 15N NMR relaxation experiments to probe, for the glycosylated human CD2 adhesion domain, the overall molecular motion, as well as very fast nanosecond-picosecond (ns-ps) and slow millisecond-microsecond (ms-microsecond) internal motions. Using a novel analysis method that considers all residues, we obtained a correlation time for the overall motion of 9.5 +/- 0.3 ns. Surprisingly, we found a large contiguous patch of residues in the counterreceptor (CD58) binding site of human CD2 exhibiting slow conformational exchange motions (ms-microsecond). On the other hand, almost none of the residues of the CD58 binding side display fast (ns-ps) internal motions of amplitudes larger than what is seen for well-ordered regions of the structure. Residues close to the N-glycosylation site, and the first N-acetylglucosamine of the high mannose glycan are as rigid as the protein core. Residues conserved in the immunoglobulin superfamily V-set domain are generally very rigid.
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