1A4J

DIELS ALDER CATALYTIC ANTIBODY GERMLINE PRECURSOR

Summary for 1A4J

• Entry DOI: 10.2210/pdb1a4j/pdb
• Descriptor: IMMUNOGLOBULIN, DIELS ALDER CATALYTIC ANTIBODY (LIGHT CHAIN), IMMUNOGLOBULIN, DIELS ALDER CATALYTIC ANTIBODY (HEAVY CHAIN) (3 entities in total)
• Functional Keywords: immunoglobulin, antibody, catalytic antibody, diels alder, germline
• Biological source: Mus musculus (house mouse); More
• Cellular location: Secreted : P01834
• Total number of polymer chains: 4
• Total formula weight: 94599.87

Authors

Spiller, B.W.,Romesburg, F.E.,Schultz, P.G.,Stevens, R.C. (deposition date: 1998-01-30, release date: 1998-05-13, Last modification date: 2024-10-30)

Primary citation

Romesberg, F.E.,Spiller, B.,Schultz, P.G.,Stevens, R.C.
Immunological origins of binding and catalysis in a Diels-Alderase antibody.
Science, 279:1929-1933, 1998

PubMed Abstract: The three-dimensional structure of an antibody (39-A11) that catalyzes a Diels-Alder reaction has been determined. The structure suggests that the antibody catalyzes this pericyclic reaction through a combination of packing and hydrogen-bonding interactions that control the relative geometries of the bound substrates and electronic distribution in the dienophile. A single somatic mutation, serine-91 of the light chain to valine, is largely responsible for the increase in affinity and catalytic activity of the affinity-matured antibody. Structural and functional studies of the germ-line precursor suggest that 39-A11 and related antibodies derive from a family of germ-line genes that have been selected throughout evolution for the ability of the encoded proteins to form a polyspecific combining site. Germ line-encoded antibodies of this type, which can rapidly evolve into high-affinity receptors for a broad range of structures, may help to expand the binding potential associated with the structural diversity of the primary antibody repertoire.

PubMed: 9506942
DOI: 10.1126/science.279.5358.1929

Experimental method

X-RAY DIFFRACTION (2.1 Å)