1YED
STRUCTURE OF A CATALYTIC ANTIBODY IGG2A FAB FRAGMENT (D2.4)
Summary for 1YED
| Entry DOI | 10.2210/pdb1yed/pdb |
| Descriptor | IGG1 FAB FRAGMENT (D.2.4), 4-NITRO-BENZYLPHOSPHONOBUTANOYL-GLYCINE, ... (4 entities in total) |
| Functional Keywords | catalytic antibody, transition state analogue |
| Biological source | Mus musculus (house mouse) More |
| Cellular location | Isoform Secreted: Secreted: P01868 |
| Total number of polymer chains | 4 |
| Total formula weight | 97905.56 |
| Authors | Golinelli-Pimpaneau, B.,Knossow, M. (deposition date: 1997-04-15, release date: 1997-10-15, Last modification date: 2024-11-06) |
| Primary citation | Charbonnier, J.B.,Golinelli-Pimpaneau, B.,Gigant, B.,Tawfik, D.S.,Chap, R.,Schindler, D.G.,Kim, S.H.,Green, B.S.,Eshhar, Z.,Knossow, M. Structural convergence in the active sites of a family of catalytic antibodies. Science, 275:1140-1142, 1997 Cited by PubMed Abstract: The x-ray structures of three esterase-like catalytic antibodies identified by screening for catalytic activity the entire hybridoma repertoire, elicited in response to a phosphonate transition state analog (TSA) hapten, were analyzed. The high resolution structures account for catalysis by transition state stabilization, and in all three antibodies a tyrosine residue participates in the oxyanion hole. Despite significant conformational differences in their combining sites, the three antibodies, which are the most efficient among those elicited, achieve catalysis in essentially the same mode, suggesting that evolution for binding to a single TSA followed by screening for catalysis lead to antibodies with structural convergence. PubMed: 9027317DOI: 10.1126/science.275.5303.1140 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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