The metastasis suppressor KISS1 is an intrinsically disordered protein slightly more extended than a random coil.

ABSTRACT: The metastasis suppressor KISS1 is reported to be involved in the progression of several solid neoplasias, making it a promising molecular target for controlling their metastasis. The KISS1 sequence contains an N-terminal secretion signal and several dibasic sequences that are proposed to be the proteolytic cleavage sites. We present the first structural characterization of KISS1 by circular dichroism, multi-angle light scattering, small angle X-Ray scattering and NMR spectroscopy. An analysis of the KISS1 backbone NMR chemical shifts does not reveal any preferential conformation and deviation from a random coil ensemble. The backbone 15N transverse relaxation times indicate a mildly reduced mobility for two regions that are rich in bulky residues. The small angle X-ray scattering curve of

SUBMITTER: Ibanez de Opakua A 

PROVIDER: S-EPMC5313212 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature