Disulfide mutants of the binding domain of the rat low affinity nerve growth factor receptor (p75NGFR).

Abstract

The binding domain of the low affinity nerve growth factor receptor (p75NGFR) is built from four "cysteine repeats," with almost identical patterns of half-cystine residues. To study the pattern of disulfide bridging within each cysteine repeat, we have mutated pairs of cysteine residues, primarily in the fourth repeat, and have tested the relative ability… (More)

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