User:Gabriel Zarzana Espinoza/Sandbox 1

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Function

The transforming growth factor beta 1 receptor is a protein that initiates the action signal of this factor by phosphorylating cytoplasmic proteins Smads at the C-terminus, causing these proteins to form a heteromeric complex. This complex will move to the nucleus to regulate the transcription of some specific genes of this factor, such as genes for: proliferation, differentiation, apoptosis or cell migration and the development of fibrosis in several organs, among others. This receptor is the product of the translation and transcription of the TGFBR1 gene, also known as ALK5, which is located on chromosome 9 of organisms belonging to the species Homo sapiens.

Disease

Small inhibitory molecules can block the catalytic activity of this protein by binding to its kinase through hydrogen bonds or hydrophobic interactions. These molecules, which generally have a central imidazole core with a pyridine ring, can be used on ALK5 to reduce pathological fibrosis induced by this receptor. ALK5 inhibitory substances can also be used to treat cancer (NEED REFERENCE FOR THIS).

Relevance

Structural highlights

This protein is an activin-type kinase receptor belonging to the heterotetrameric receptor complex, also constituted by the beta 2 receptor (perhaps reformulating this phrase so that it is understood that the heterotetrameric complex is composed of 2 beta 1 receptors and two beta 2 receptors), to which the transforming growth factor binds. This beta 1 receptor has a similar structure to that of the beta 2 receptor, with both being transmembrane serine / threonine kinase receptors and having: an extracellular cysteine-rich N-terminal domain involved in ligand binding; a transmembrane helix; and a C-terminal cytoplasmic kinase domain. In addition, ALK5 also has a regulatory segment called the GS region or domain. This domain is located upstream of the catalytic kinase domain and has a conserved sequence of 185TTSGSGSGLP194 at its center. This region is phosphorylated in its serine and threonine residues by the beta 2 receptor of the heterotetrameric complex, when it is linked to the growth factor. Thus, the beta 1 receptor is activated and, in turn, transmits the factor signal when phosphorylating, and thus activating, Smad transcription factors.

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