Literature DB >> 1568482

A predicted three-dimensional structure for the carcinoembryonic antigen (CEA).

P A Bates1, J Luo, M J Sternberg.   

Abstract

A three-dimensional model for the carcinoembryonic antigen (CEA) has been constructed by knowledge-based computer modelling. Each of the seven extracellular domains of CEA are expected to have immunoglobulin folds. The N-terminal domain of CEA was modelled using the first domain of the recently solved NMR structure of rat CD2, as well as the first domain of the X-ray crystal structure of human CD4 and an immunoglobulin variable domain REI as templates. The remaining domains were modelled from the first and second domains of CD4 and REI. Link conformations between the domains were taken from the elbow region of antibodies. A possible packing model between each of the seven domains is proposed. Each residue of the model is labelled as to its suitability for site-directed mutagenesis.

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Year:  1992        PMID: 1568482     DOI: 10.1016/0014-5793(92)81249-l

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  18 in total

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4.  A role for naturally occurring variation of the murine coronavirus spike protein in stabilizing association with the cellular receptor.

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5.  Evidence for regulated dimerization of cell-cell adhesion molecule (C-CAM) in epithelial cells.

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Review 9.  Biological therapy: approaches in colorectal cancer. Strategies to enhance carcinoembryonic antigen (CEA) as an immunogenic target.

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10.  Homophilic adhesion between Ig superfamily carcinoembryonic antigen molecules involves double reciprocal bonds.

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Journal:  J Cell Biol       Date:  1993-08       Impact factor: 10.539

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