A disordered encounter complex is central to the yeast Abp1p SH3 domain binding pathway.

ABSTRACT: Protein-protein interactions are involved in a wide range of cellular processes. These interactions often involve intrinsically disordered proteins (IDPs) and protein binding domains. However, the details of IDP binding pathways are hard to characterize using experimental approaches, which can rarely capture intermediate states present at low populations. SH3 domains are common protein interaction domains that typically bind proline-rich disordered segments and are involved in cell signaling, regulation, and assembly. We hypothesized, given the flexibility of SH3 binding peptides, that their binding pathways include multiple steps important for function. Molecular dynamics simulations were used to characterize the steps of binding between the yeast Abp1p SH3 domain (AbpSH3) and a proline-r

SUBMITTER: Gerlach GJ 

PROVIDER: S-EPMC7514057 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature