1AXT
IMMUNE VERSUS NATURAL SELECTION: ANTIBODY ALDOLASES WITH THE RATES OF NATURAL ENZYMES
1AXT の概要
エントリーDOI | 10.2210/pdb1axt/pdb |
分子名称 | IMMUNOGLOBULIN IGG2A (3 entities in total) |
機能のキーワード | immunoglobulin, antibody fab', catalyst, aldolase reaction |
由来する生物種 | Mus musculus (house mouse) 詳細 |
細胞内の位置 | Cell membrane; Single-pass membrane protein (Potential): P01865 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 47626.31 |
構造登録者 | |
主引用文献 | Barbas 3rd., C.F.,Heine, A.,Zhong, G.,Hoffmann, T.,Gramatikova, S.,Bjornestedt, R.,List, B.,Anderson, J.,Stura, E.A.,Wilson, I.A.,Lerner, R.A. Immune versus natural selection: antibody aldolases with enzymic rates but broader scope. Science, 278:2085-2092, 1997 Cited by PubMed Abstract: Structural and mechanistic studies show that when the selection criteria of the immune system are changed, catalytic antibodies that have the efficiency of natural enzymes evolve, but the catalytic antibodies are much more accepting of a wide range of substrates. The catalytic antibodies were prepared by reactive immunization, a process whereby the selection criteria of the immune system are changed from simple binding to chemical reactivity. This process yielded aldolase catalytic antibodies that approximated the rate acceleration of the natural enzyme used in glycolysis. Unlike the natural enzyme, however, the antibody aldolases catalyzed a variety of aldol reactions and decarboxylations. The crystal structure of one of these antibodies identified the reactive lysine residue that was selected in the immunization process. This lysine is deeply buried in a hydrophobic pocket at the base of the binding site, thereby accounting for its perturbed pKa. PubMed: 9405338DOI: 10.1126/science.278.5346.2085 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.15 Å) |
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