SH3 Domain Binding Glutamic Acid-Rich Protein Like Human Recombinant
SH3 Domain Binding Glutamic Acid-Rich Protein Like 2 Human Recombinant
SH3 Domain Binding Glutamic Acid-Rich Protein Like 3 Human Recombinant
SH3-domain GRB2-like 2 Human Recombinant
SH3-domain GRB2-like endophilin B1 Human Recombinant
SH3-domain GRB2-like endophilin B2 Human Recombinant
The SRC Homology 3 (SH3) domain is a small protein domain consisting of approximately 60 amino acid residues. It was initially identified as a conserved sequence in the viral adaptor protein v-Crk. SH3 domains are present in various proteins, including phospholipase and several cytoplasmic tyrosine kinases such as Abl and Src . They are found in proteins involved in signaling pathways that regulate the cytoskeleton, Ras protein, and Src kinase . SH3 domains are classified based on their ability to bind to proline-rich motifs (PRMs) and are found in both eukaryotic and prokaryotic organisms .
SH3 domains exhibit a characteristic beta-barrel fold consisting of five or six β-strands arranged as two tightly packed anti-parallel β sheets . They are involved in protein-protein interactions and mediate the assembly of specific protein complexes by binding to proline-rich peptides . SH3 domains are expressed in various tissues and are involved in numerous cellular processes, including cell survival, proliferation, differentiation, migration, and polarity .
The primary biological function of SH3 domains is to facilitate transient protein-protein interactions by selectively interacting with proline-rich motifs . They play a crucial role in immune responses and pathogen recognition by mediating the assembly of protein complexes involved in these processes . SH3 domains are also implicated in the regulation of cytoskeletal dynamics, cell signaling, and cellular communication .
SH3 domains interact with other molecules and cells through their ability to bind to proline-rich motifs in their binding partners . This interaction is mediated by the hydrophobic pocket of the SH3 domain, which binds to the proline-rich sequence . SH3 domains are involved in downstream signaling cascades by regulating the interactions of proteins involved in cytoplasmic signaling . They also play a role in the regulation of important cellular pathways, such as cell proliferation, migration, and cytoskeletal modifications .
The expression and activity of SH3 domains are regulated by various mechanisms, including transcriptional regulation and post-translational modifications . Phosphorylation of tyrosine residues within the SH3 domain can act as a regulatory switch, controlling the binding affinity of the SH3 domain to its interacting partners . This regulation allows SH3 domains to adopt different conformations and interact with various proteins, thereby modulating their activity and function .
SH3 domains have numerous applications in biomedical research, diagnostic tools, and therapeutic strategies . They are used as models to study protein-protein interactions and the mechanisms of aggregation and specificity of interactions . SH3 domains are also attractive drug targets due to their involvement in various cellular processes, such as migration, invasiveness, and actin reorganization . High-affinity peptides that bind SH3 domains are being developed as candidates for anticancer treatment .
SH3 domains play a significant role throughout the life cycle, from development to aging and disease . They are involved in the regulation of cellular processes essential for development, such as cell survival, proliferation, and differentiation . SH3 domains also play a role in aging and disease by regulating the interactions of proteins involved in cellular signaling and communication . Their dysregulation can lead to various diseases, including cancer, leukemia, osteoporosis, Alzheimer’s disease, and infections .