PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 8263940

Shape complementarity at protein/protein interfaces.

M C Lawrence·P M Colman
View original source ↗Export metadata ↓

Abstract

A new statistic Sc, which has a number of advantages over other measures of packing, is used to examine the shape complementarity of protein/protein interfaces selected from the Brookhaven Protein Data Bank. It is shown using Sc that antibody/antigen interfaces as a whole exhibit poorer shape complementarity than is observed in other systems involving protein/protein interactions. This result can be understood in terms of the fundamentally different evolutionary history of particular antibody/antigen associations compared to other systems considered, and in terms of the differing chemical natures of the interfaces.

Explore related subjects

Antigen-Antibody ReactionsHemoglobinsImmunoglobulin Fab FragmentsMacromolecular SubstancesModels, MolecularNeuraminidaseProtein BindingProtein ConformationProteinsJournal Article

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

M C Lawrence, P M Colman. 1993-12-20. Shape complementarity at protein/protein interfaces.. https://doi.org/10.1006/jmbi.1993.1648

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2000

Flow immunochemical bio-recognition detection for the determination of interleukin-10 in cell samples.

On- and off-line heterogeneous non-competitive flow immunoassays for the determination of Interleukin-10 are described. The sample containing IL-10 is mixed, either on-line in a reaction coil or off-line in a test tube, with fluorescent labelled anti-IL-10 antibodies to form an antibody-antigen complex. The labelled unbound antibodies are trapped on an immobilized IL-10 column whereas the IL-10-antibody complexes are eluted and detected downstream by a fluorescence detector. The optimization of the systems was performed with respect to choice of affinity support, flow rate, carrier buffer additives, pH and antibody-antigen association. Both bio recognition assays were tested with a spiked cell medium and the IL-10 detection limits in this matrix was found to be 8 fmol using the off-line incubation mode and 40 fmol using the on-line incubation mode. The sample through-put was 26 and 40 samples per hour in the on-line and off-line incubation modes, respectively. IL-10 identification in the sample fractions was achieved using MALDI-TOF MS.

Antigen-Antibody Reactions↗
PubMed2000

Integration of an immunosorbent assay system: analysis of secretory human immunoglobulin A on polystyrene beads in a microchip.

An immunosorbent assay system was integrated into a glass microchip. Polystyrene beads were introduced into a microchannel, and then human secretory immunoglobulin A (s-IgA) adsorbed on the bead surface was reacted with colloidal gold conjugated anti-s-IgA antibody and detected by a thermal lens microscope. The scale merits of liquid microspace on the molecular behavior remarkably contributed to reduced assay time. The integration cut the time necessary for the antigen-antibody reaction by 1/90, thus shortening the overall analysis time from 24 h to less than 1 h. Moreover, troublesome operations required for conventional immunosorbent assays could be replaced by simple operations.

Antigen-Antibody Reactions↗