Typical area of interaction between receptor and a portion of the antigen (called epitope)

Value 600 Å^2
Organism Unspecified
Reference Alan S. Perelson, Ge´rard Weisbuch, Immunology for physicists, Rev. Mod. Phys. 69, 1219–1268 (1997) p.1222 right column top paragraph
Primary Source Amit AG, Mariuzza RA, Phillips SE, Poljak RJ. Three-dimensional structure of an antigen-antibody complex at 2.8 A resolution. Science. 1986 Aug 15 233(4765):747-53.& Ajitkumar P et al., Evidence that multiple residues on both the alpha-helices of the class I MHC molecule are simultaneously recognized by the T cell receptor. Cell. 1988 Jul 1 54(1):47-56.PubMed ID2426778, 3260136
Comments "Recognition in the immune system occurs at the molecular level and is based on the complementarity in shape between the binding site of the receptor and a portion of the antigen called an epitope (see Fig. 2). The interaction between the receptor and the epitope is noncovalent and usually involves van der Waals forces, interactions among charged groups, and hydrogen bonds. These weak interactions are nevertheless strong enough to keep the macromolecules bound when the area of interaction is sufficiently large. Typical areas of interaction are 600 Å^2 (primary sources)."
Entered by Uri M
ID 109929