SAXS/MC studies of the mixed-folded protein Cdt1 reveal monomeric, folded over conformations.

ABSTRACT: Cdt1 is a protein critical for DNA replication licensing and is well-established to be a binding partner of the minichromosome maintenance (MCM) complex. Cdt1 has also been demonstrated to have an emerging, "moonlighting" role at the kinetochore via direct binding to microtubules and to the Ndc80 complex. However, it is not known how the structure and conformations of Cdt1 could allow for these multiple, completely unique sets of protein complexes. And while there exist multiple robust methods to study entirely folded or entirely unfolded proteins, structure-function studies of combined, mixed folded/disordered proteins remain challenging. It this work, we employ multiple orthogonal biophysical and computational techniques to provide a detailed structural characterization of human Cdt1 92-

SUBMITTER: Smith KP 

PROVIDER: S-EPMC10802334 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature