TGF alpha

1GK5, 1MOX, 1YUF, 1YUG, 2TGF, 3E50, 3TGF, 4TGF703921802ENSG00000163235ENSMUSG00000029999P01135P48030NM_001099691NM_001308158NM_001308159NM_003236NM_031199NP_001093161NP_001295087NP_001295088NP_003227NP_112476Transforming growth factor alpha (TGF-α) is a protein that in humans is encoded by the TGFA gene. As a member of the epidermal growth factor (EGF) family, TGF-α is a mitogenic polypeptide. The protein becomes activated when binding to receptors capable of protein kinase activity for cellular signaling.1mox: Crystal Structure of Human Epidermal Growth Factor Receptor (residues 1-501) in complex with TGF-alpha1yuf: TYPE ALPHA TRANSFORMING GROWTH FACTOR, NMR, 16 MODELS WITHOUT ENERGY MINIMIZATION1yug: TYPE ALPHA TRANSFORMING GROWTH FACTOR, NMR, 15 MODELS AFTER ECEPP/3 ENERGY MINIMIZATION2tgf: THE SOLUTION STRUCTURE OF HUMAN TRANSFORMING GROWTH FACTOR ALPHA3tgf: THE SOLUTION STRUCTURE OF HUMAN TRANSFORMING GROWTH FACTOR ALPHA4tgf: SOLUTION STRUCTURES OF HUMAN TRANSFORMING GROWTH FACTOR ALPHA DERIVED FROM 1*H NMR DATA Transforming growth factor alpha (TGF-α) is a protein that in humans is encoded by the TGFA gene. As a member of the epidermal growth factor (EGF) family, TGF-α is a mitogenic polypeptide. The protein becomes activated when binding to receptors capable of protein kinase activity for cellular signaling. TGF-α is a transforming growth factor that is a ligand for the epidermal growth factor receptor, which activates a signaling pathway for cell proliferation, differentiation and development. This protein may act as either a transmembrane-bound ligand or a soluble ligand. This gene has been associated with many types of cancers, and it may also be involved in some cases of cleft lip/palate. TGF-α is synthesized internally as part of a 160 (human) or 159 (rat) amino acid transmembrane precursor. The precursor is composed of an extracellular domain containing a hydrophobic transmembrane domain, 50 amino acids of TGF-α, and a 35-residue-long cytoplasmic domain. In its smallest form, TGF-α has six cysteines linked together via three disulfide bridges. Collectively, all members of the EGF/TGF-α family share this structure. The protein, however, is not directly related to TGF-β. Limited success has resulted from attempts to synthesize of a reductant molecule to TGF-α that displays a similar biological profile. In the stomach, TGF-α is manufactured within the normal gastric mucosa. TGF-α has been shown to inhibit gastric acid secretion. TGF-α can be produced in macrophages, brain cells, and keratinocytes. TGF-α induces epithelial development. Considering that TGF-α is a member of the EGF family, the biological actions of TGF-α and EGF are similar. For instance, TGF-α and EGF bind to the same receptor. When TGF-α binds to EGFR it can initiate multiple cell proliferation events. Cell proliferation events that involve TGF-α bound to EGFR include wound healing and embryogenesis. TGF-α is also involved in tumerogenesis and believed to promote angiogenesis. TGF-α has also been shown to stimulate neural cell proliferation in the adult injured brain. A 170-kDa glycosylated protein known as the EGF receptor binds to TGF-α allowing the polypeptide to function in various signaling pathways. The EGF receptor is characterized by having an extracellular domain that has numerous amino acid motifs. EGFR is essential for a single transmembrane domain, an intracellular domain (containing tyrosine kinase activity), and ligand recognition. As a membrane anchored-growth factor, TGF-α can be cleaved from an integral membrane glycoprotein via a protease. Soluble forms of TGF-α resulting from the cleavage have the capacity to activate EGFR. EGFR can be activated from a membrane-anchored growth factor as well.