Segal D M, Padlan E A, Cohen G H, Rudikoff S, Potter M, Davies D R
Proc Natl Acad Sci U S A. 1974 Nov;71(11):4298-302. doi: 10.1073/pnas.71.11.4298.
The structure of the Fab of McPC 603, a mouse myeloma protein with phosphorylcholine binding activity, has been determined to 3.1-A resoltuion. The four domains are found to be structurally similar with a well-defined double-layer structure. A large cavity exists at one end of the fragment, the walls of which are formed exclusively of hypervariable residues. Phosphorylcholine binds in this cavity and forms specific interactions with several well-defined amino-acid side chains of the protein. The hapten is bound asymmetrically and interacts more with the heavy chain than with the light chain.
具有磷酸胆碱结合活性的小鼠骨髓瘤蛋白McPC 603的Fab片段结构已确定,分辨率达3.1埃。发现四个结构域在结构上相似,具有明确的双层结构。片段一端存在一个大腔,其壁完全由高变残基形成。磷酸胆碱结合在这个腔内,并与蛋白质的几个明确的氨基酸侧链形成特异性相互作用。半抗原以不对称方式结合,与重链的相互作用比对轻链的更多。