Sandbox Reserved 1726: Difference between revisions

Unlike the poly-Glycine helices, the <scene name='90/904331/Egf_like_domain/3'>Epidermal Growth Factor-like Domain</scene> is malleable and repositioning of this domain is essential for activation of the protein.<ref name="Reshetnyak" /> This domain undergoes conformational changes upon ligand binding and when in contact with the TNF-like domain.<ref name="Reshetnyak" /> The <scene name='90/904332/Tnf_egf_interface/3'>interface between the EGF-like and TNF-like domains</scene> consists of primarily hydrophobic residues, which enables their flexibility with regards to one another.<ref name="Reshetnyak" /> Hydrogen bonding occurs mostly between residues on the TNF-like domain.<ref name="Reshetnyak" /> There is only one hydrogen bond between the domains that is between residues Y734 on the TNF-like interface and Y984 on the EGF-interface.<ref name="Reshetnyak" /> Major motifs in the EGF-like domain are major and minor β-hairpins, which are stabilized by 3 conserved disulfide bridges. <ref name="Reshetnyak" /> The major β-hairpins in the EGF-like domain interact with the ALKAL2 helices after ALKAL2 binding <ref name="Reshetnyak" />.