Structural models for carcinoembryonic antigen and its complex with the single‐chain Fv antibody molecule MFE23

FEBS Letters

Perkins, Stephen J.¹  Boehm, Mark K.¹ 

[1]Department of Biochemistry and Molecular Biology, Royal Free Campus, Royal Free and University College Medical School, University College London, Rowland Hill St., London NW3 2PF, UK

关键词: Antibody;    Carcinoembryonic antigen;    Homology model;    Structure prediction;    Scattering;    Single-chain Fv;    CEA;    carcinoembryonic antigen;    CEA-1 to CEA-7;    domain numbering in CEA;    H1-H120 and L1-L106;    sequence numbering of MFE23 heavy and light chains respectively;    H1-H3 and L1-L3;    antigen-binding loops of MFE23;    ICAM-2;    intercellular cell adhesion molecule-2;    Ig;    immunoglobulin;    PDB;    protein data bank;    VH;    variable heavy chain domain;    VL;    variable light chain domain;    VCAM-1;    vascular cell adhesion molecule;   

DOI  :  10.1016/S0014-5793(00)01612-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

MFE23 is a single chain Fv antibody that has a high affinity for carcinoembryonic antigen (CEA). A full homology model for CEA based on V-type, I-type and C2-type immunoglobulin folds, 28 oligosaccharides and the interdomain angle of CD2 was validated using solution scattering data. The superimposition of the intermolecular contacts observed in our recent crystal structure of MFE23 with the N-terminal domain of CEA permitted the MFE23–CEA complex to be modelled. Good surface and electrostatic complementarity and carbohydrate-unhindered access of MFE23 with the indentation between the first two CEA domains was observed. The model is supported by biochemical data and provides insight on the high affinity of MFE23 for CEA.

【 授权许可】

Unknown