Zdanov A, Li Y, Bundle D R, Deng S J, MacKenzie C R, Narang S A, Young N M, Cygler M
Biotechnology Research Institute, National Research Council of Canada, Montreal, PQ.
Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6423-7. doi: 10.1073/pnas.91.14.6423.
We describe here the 1.7-A resolution structure of a single-chain antibody variable domain (scFv) molecule, based on the carbohydrate-binding antibody Se155-4, complexed with the trisaccharide ligand alpha-D-Gal(1-->2)[alpha-D-Abe(1-->3)]alpha-D-Manp1-->OMe, where Abe is abequose. The scFv expressed in Escherichia coli has the variable region light chain to heavy chain polarity with the domains connected by a 19-residue linker. Although the linker is partially disordered in the crystal, the packing of the molecules suggests a monomeric state of the scFv. The carbohydrate adopts a different conformation about the Man-Gal linkage than was observed previously in the Fab-trisaccharide complex. Instead of a direct hydrogen bond between O2Abe and O2Gal, these two atoms are bridged by a water molecule in the present complex.
我们在此描述了基于碳水化合物结合抗体Se155-4的单链抗体可变结构域（scFv）分子的1.7埃分辨率结构，该分子与三糖配体α-D-半乳糖（1→2）[α-D-阿比可糖（1→3）]α-D-甘露糖-1→OMe复合，其中阿比可糖为阿比糖。在大肠杆菌中表达的scFv具有可变区轻链到重链的极性，结构域由一个19个残基的连接子连接。尽管连接子在晶体中部分无序，但分子的堆积表明scFv处于单体状态。碳水化合物在甘露糖-半乳糖连接上采取了与先前在Fab-三糖复合物中观察到的不同构象。在当前复合物中，O2阿比糖和O2半乳糖之间不是直接形成氢键，而是由一个水分子将这两个原子连接起来。
