Multiple structural states in an intrinsically disordered protein, SNAP-25, using circular dichroism.

ABSTRACT: SNAP-25, together with other SNARE proteins, drives fusion of synaptic vesicles with the nerve cell membrane, leading to neurotransmitter release. It is unique in contributing two α helices to the four-helix bundle known as the SNARE complex. Complex formation drives fusion as these proteins transform from a disordered to ordered (coiled-coil) state. SNAP-25 has two isoforms, -25A and -25B, but little is known of any structural differences, nor are there extensive reports of the structures of its two helical domains, SN1 and SN2. Thus, the benefit of having two distinct isoforms of SNAP-25, each with two distinct domains, is unknown. Here, we use circular dichroism spectroscopy and mass spectrometry to further characterize the secondary structure of SNAP-25A, SNAP-25B, SN1, SN2, and a cyst

SUBMITTER: Sumsion JS 

PROVIDER: S-EPMC12256890 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature