Biochemistry. 1992 May 12;31(18):4431-6.

Dimeric structure and conformational stability of brain-derived neurotrophic factor and neurotrophin-3.

Radziejewski C, Robinson RC, DiStefano PS, Taylor JW.

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Regeneron Pharmaceuticals Inc., Tarrytown, New York 10591.

Abstract

We have examined the molecular structure of the related neurotrophic factors brain-derived neurotrophic factor (BDNF) and neurotrophin-3 (NT-3) by physical methods, including gel filtration, velocity sedimentation, sedimentation equilibrium, urea gel electrophoresis, fluorescence spectroscopy, and far-ultraviolet circular dichroism. The results of these studies indicate that at physiologically relevant concentrations both recombinant proteins exist as tightly associated dimers. The dimers are stable even in 8 M solutions of urea. In solutions of guanidine hydrochloride, BDNF and NT-3 undergo slow unfolding between 3 and 5 M concentration of denaturant. Circular dichroism spectroscopy revealed approximately 70% beta-sheet and 20% beta-turn content in the native structure of both neurotrophic factors. In this respect, BDNF and NT-3 resemble other polypeptide growth factors whose receptors are also integral protein-tyrosine kinases.

PMID:: 1581298; [PubMed - indexed for MEDLINE]

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