IGF1: Difference between revisions
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The coding RNA of this protein creates 4 isoforms differing from each other due to RNA splicing. | The coding RNA of this protein creates 4 isoforms differing from each other due to RNA splicing. | ||
Nevertheless, all 4 of them have cysteine residues that are able to make disulfide bond. This enable them to link to IGF-1 receptor. | Nevertheless, all 4 of them have cysteine residues that are able to make disulfide bond. This enable them to link to IGF-1 receptor. | ||
Its secondary structure as shown here is composed of alpha helix and beta strand. | |||
[[Image:IGF1.png]] | [[Image:IGF1.png]] | ||
Its 3D structure is : <Structure load='https://www.swissmodel.expasy.org/templates/3lri.1?_ga=1.140471216.2002904762.1485367069' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | |||
=== Stimulating interaction : IGF1 - IGF1R === | === Stimulating interaction : IGF1 - IGF1R === | ||
IGF1R is a transmembrane protein receptor. It is composed of two alpha subunits and two tyrosine beta subunits. Both alpha subunits are cysteine-rich region and therefore linked with a disulfide bond. Ligand-binding on alpha subunit induces activation of beta subunit by autophosphorylation. It further leads to activation of the Akt and mTor pathways inside the cell. | IGF1R is a transmembrane protein receptor. It is composed of two alpha subunits and two tyrosine beta subunits. Both alpha subunits are cysteine-rich region and therefore linked with a disulfide bond. Ligand-binding on alpha subunit induces activation of beta subunit by autophosphorylation. It further leads to activation of the Akt and mTor pathways inside the cell. | ||
