Expression and structure of the human NGF receptor |
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Authors: | D Johnson A Lanahan C R Buck A Sehgal C Morgan E Mercer M Bothwell M Chao |
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Affiliation: | 1. Centre for Stem Cell Research, A Unit of inStem Bengaluru, Christian Medical College Campus, Bagayam, Vellore, Tamil Nadu, India;2. Cytogenetics Unit, Christian Medical College, Vellore, Tamil Nadu, India;3. Department of General Pathology, Christian Medical College, Vellore, Tamil Nadu, India;4. Department of Transfusion Medicine and Immunohematology, Christian Medical College, Vellore, Tamil Nadu, India;5. Department of Hematology, Christian Medical College, Vellore, Tamil Nadu, India;1. Department of Hematology, The First Affiliated Hospital of Xiamen University and Institute of Hematology, School of Medicine, Xiamen University, Xiamen 361003, P.R. China;2. Eye Institute and Xiamen Eye Center Affiliated to Xiamen University, Xiamen 361001, China;3. Department of Pathology, The First Affiliated Hospital of Xiamen University, Xiamen 361003, China;4. Department of Hematology and Rheumatology, Longyan First Hospital, Affiliated to Fujian Medical University, Longyan 364000, P.R. China;1. Department of Immunology, Institute for Biological Research “Siniša Stanković”, University of Belgrade, Belgrade, Serbia;2. Institute of Microbiology and Immunology, School of Medicine, University of Belgrade, Belgrade, Serbia |
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Abstract: | The nucleotide sequence for the human nerve growth factor (NGF) receptor has been determined. The 3.8 kb receptor mRNA encodes a 427 amino acid protein containing a 28 amino acid signal peptide, an extracellular domain containing four 40 amino acid repeats with six cysteine residues at conserved positions followed by a serine/threonine-rich region, a single transmembrane domain, and a 155 amino acid cytoplasmic domain. The sequence of the extracellular domain of the NGF receptor predicts a highly ordered structure containing a negatively charged region that may serve as the ligand-binding site. This domain is conserved through evolution. Transfection of a full-length cDNA in mouse fibroblasts results in stable expression of NGF receptors that are recognized by monoclonal antibodies to the human NGF receptor and that bind [125I]NGF. |
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