NERVE GROWTH-FACTOR BINDING DOMAIN OF THE NERVE GROWTH-FACTOR RECEPTOR

作者：WELCHER AA^*; BITLER CM; RADEKE MJ; SHOOTER EM

来源：Proceedings of the National Academy of Sciences of the United States of America, 1991, 88(1): 159-163.

DOI：10.1073/pnas.88.1.159

• NEUROTROPHIC FACTORS
• MUTAGENESIS
• CROSS-LINKING

A structural analysis of the rat low-affinity nerve growth factor (NGF) receptor was undertaken to define the NGF binding domain. Mutant NGF receptor DnA constructs were expressed in mouse fibroblasts or COS cells, and the ability of the mutant receptors to bind NGF was assayed. In the first mutant, all but 16 amino acid residues of the intracellular domain of the receptor were removed. This receptor bound NGF with a K(d) comparable to that of the wild-type receptor. A second mutant contained only the four cysteine-rich sequences from the extracellular portion of the protein. This mutant was expressed in COS cells and the resultant protein was a secreted soluble form of the receptor that was able to bind NGF. Two N-terminal deletions, in which either the first cysteine-rich sequences were removed, bound NGF. However, a mutant lacking all four cysteine-rich sequences was unable to bind NGF. These results show that the four cysteine-rich sequences of the NGF receptor contain the NGF binding domain.

• 出版日期1991-1