Structural highlights
Function
[CEAM5_HUMAN] Cell surface glycoprotein that plays a role in cell adhesion and in intracellular signaling. Receptor for E.coli Dr adhesins.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structural models for carcinoembryonic antigen and its complex with the single-chain Fv antibody molecule MFE23.,Boehm MK, Perkins SJ FEBS Lett. 2000 Jun 9;475(1):11-6. PMID:10854848[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Taheri M, Saragovi U, Fuks A, Makkerh J, Mort J, Stanners CP. Self recognition in the Ig superfamily. Identification of precise subdomains in carcinoembryonic antigen required for intercellular adhesion. J Biol Chem. 2000 Sep 1;275(35):26935-43. PMID:10864933 doi:10.1074/jbc.M909242199
- ↑ Boehm MK, Perkins SJ. Structural models for carcinoembryonic antigen and its complex with the single-chain Fv antibody molecule MFE23. FEBS Lett. 2000 Jun 9;475(1):11-6. PMID:10854848
