Structural, in silico, and functional analysis of a Disabled-2-derived peptide for recognition of sulfatides.

ABSTRACT: Disabled-2 (Dab2) is an adaptor protein that regulates the extent of platelet aggregation by two mechanisms. In the first mechanism, Dab2 intracellularly downregulates the integrin α_IIbβ₃ receptor, converting it to a low affinity state for adhesion and aggregation processes. In the second mechanism, Dab2 is released extracellularly and interacts with the pro-aggregatory mediators, the integrin α_IIbβ₃ receptor and sulfatides, blocking their association to fibrinogen and P-selectin, respectively. Our previous research indicated that a 35-amino acid region within Dab2, which we refer to as the sulfatide-binding peptide (SBP), contains two potential sulfatide-binding motifs represented by two consecutive polybasic regions. Using molecular docking, nu

SUBMITTER: Song W 

PROVIDER: S-EPMC7421900 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature