1e07

Model of human carcinoembryonic antigen by homology modelling and curve-fitting to experimental solution scattering data

spinqualitylabelsall models 1e07 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1e07 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray solution scattering Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CEAM5_HUMAN Cell surface glycoprotein that plays a role in cell adhesion and in intracellular signaling. Receptor for E.coli Dr adhesins. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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