Molecular Dynamics Simulations of Wild Type and Mutants of SAPAP in Complexed with Shank3.

ABSTRACT: Specific interactions between scaffold protein SH3 and multiple ankyrin repeat domains protein 3 (Shank3) and synapse-associated protein 90/postsynaptic density-95⁻associated protein (SAPAP) are essential for excitatory synapse development and plasticity. In a bunch of human neurological diseases, mutations on Shank3 or SAPAP are detected. To investigate the dynamical and thermodynamic properties of the specific binding between the N-terminal extended PDZ (Post-synaptic density-95/Discs large/Zonaoccludens-1) domain (N-PDZ) of Shank3 and the extended PDZ binding motif (E-PBM) of SAPAP, molecular dynamics simulation approaches were used to study the complex of N-PDZ with wild type and mutated E-PBM peptides. To compare with the experimental data, ₉₇₄QTRL₉₇₇ and ₉₆

SUBMITTER: Piao L 

PROVIDER: S-EPMC6337207 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature