Framework Region
editIn molecular biology, framework regions are a subdivision of the fragment antigen binding region (Fab) of the antibody. Located on the tips of the Y-shaped molecule, the framework regions are responsible for supporting the binding of the hypervariable region (CDR) of the Fab to the antigen.[1] The side chains of certain amino acids in the framework help facilitate the stable binding of the antibody to the antigen[2] and define the position of the CDR so they are exposed on the surface of the chain ready to bind to an antigen.[3]
The framework region is made up of 4 amino acid segments between the 3 CDR regions of the Fab. The framework region makes up about 85% of the variable region.[3] To increase its stability, the framework region has less variability in its amino acid sequences compared to the CDR. There are 4 framework regions found on each antibody located on the two variable heavy domains and the two variable light domain.
See also
editReferences
edit- ^ Ill, C. R.; Gonzales, J. N.; Houtz, E. K.; Ludwig, J. R.; Melcher, E. D.; Hale, J. E.; Pourmand, R.; Keivens, V. M.; Myers, L. (1997-08-01). "Design and construction of a hybrid immunoglobulin domain with properties of both heavy and light chain variable regions". Protein Engineering. 10 (8): 949–957. doi:10.1093/protein/10.8.949. ISSN 0269-2139. PMID 9415445.
- ^ Abès, Riad; Dutertre, Charles-Antoine; Teillaud, Jean-Luc (2009-12-01). "[Antibodies: better knowledge for a better use]". Médecine/Sciences. 25 (12): 1011–1019. doi:10.1051/medsci/200925121011. ISSN 0767-0974. PMID 20035672.
- ^ a b Elgert, Klaus (1998). Immunology: Understanding the Immune System. John Wiley & Sons, Inc. p. 63.