1UZ8

anti-Lewis X Fab fragment in complex with Lewis X

1UZ8 の概要

• エントリーDOI: 10.2210/pdb1uz8/pdb
• 関連するPDBエントリー: 1UZ6
• 分子名称: IGG FAB (IGG3, KAPPA) LIGHT CHAIN 291-2G3-A, IGG FAB (IGG3, KAPPA) HEAVY CHAIN 291-2G3-A, alpha-L-fucopyranose-(1-3)-[beta-D-galactopyranose-(1-4)]methyl 2-acetamido-2-deoxy-beta-D-glucopyranoside, ... (4 entities in total)
• 機能のキーワード: immune system, antibody, anti-carbohydrate
• 由来する生物種: MUS MUSCULUS (MOUSE); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 95086.06

構造登録者

Van Roon, A.M.M.,Pannu, N.S.,De Vrind, J.P.M.,Hokke, C.H.,Deelder, A.M.,Van Der marel, G.A.,Van Boom, J.H.,Abrahams, J.P. (登録日: 2004-03-05, 公開日: 2004-06-29, 最終更新日: 2024-10-16)

主引用文献

Van Roon, A.M.M.,Pannu, N.S.,De Vrind, J.P.M.,Van Der Marel, G.A.,Van Boom, J.H.,Hokke, C.H.,Deelder, A.M.,Abrahams, J.P.
Structure of an Anti-Lewis X Fab Fragment in Complex with its Lewis X Antigen
Structure, 12:1227-, 2004

PubMed Abstract: The Lewis X trisaccharide is pivotal in mediating specific cell-cell interactions. Monoclonal antibody 291-2G3-A, which was generated from mice infected with schistosomes, has been shown to recognize the Lewis X trisaccharide. Here we describe the structure of the Fab fragment of 291-2G3-A, with Lewis X, to 1.8 A resolution. The crystallographic analysis revealed that the antigen binding site is a rather shallow binding pocket, and residues from all six complementary determining regions of the antibody contact all sugar residues. The high specificity of the binding pocket does not result in high affinity; the K(D) determined by isothermal calorimetry is 11 microM. However, this affinity is in the same range as for other sugar-antibody complexes. The detailed understanding of the antibody-Lewis X interaction revealed by the crystal structure may be helpful in the design of better diagnostic tools for schistosomiasis and for studying Lewis X-mediated cell-cell interactions by antibody interference.

PubMed: 15242599
DOI: 10.1016/J.STR.2004.05.008

実験手法

X-RAY DIFFRACTION (1.8 Å)