1A4K
DIELS ALDER CATALYTIC ANTIBODY WITH TRANSITION STATE ANALOGUE
Summary for 1A4K
| Entry DOI | 10.2210/pdb1a4k/pdb |
| Descriptor | ANTIBODY FAB, CADMIUM ION, [4-(4-ACETYLAMINO-PHENYL)-3,5-DIOXO-4-AZA-TRICYCLO[5.2.2.0 2,6]UNDEC-1-YLCARBAMOYLOXY]-ACETIC ACID, ... (5 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 | 95960.52 |
| 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: 2024-10-23) |
| 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 Cited by 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: 9506942DOI: 10.1126/science.279.5358.1929 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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