1YEC

STRUCTURE OF A CATALYTIC ANTIBODY IGG2A FAB FRAGMENT (D2.3)

1YEC の概要

• エントリーDOI: 10.2210/pdb1yec/pdb
• 分子名称: IGG2A FAB FRAGMENT (D2.3), ZINC ION, 4-NITRO-BENZYLPHOSPHONOBUTANOYL-GLYCINE, ... (5 entities in total)
• 機能のキーワード: catalytic antibody, transition state analogue
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49013.15

構造登録者

Golinelli-Pimpaneau, B.,Knossow, M. (登録日: 1997-04-15, 公開日: 1997-10-15, 最終更新日: 2024-10-30)

主引用文献

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

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: 9027317
DOI: 10.1126/science.275.5303.1140

実験手法

X-RAY DIFFRACTION (1.9 Å)