Sandbox Reserved 830: Difference between revisions

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<scene name='56/568028/Oncostatin_bridge1/1'>The disulphide bridge between Cys6 and Cys127</scene> connects the N-terminal loop (Gly4-Glu9) preceding helix A to the C terminus of helix C. <scene name='56/568028/Oncostatine_bridge2/1'>The second disulphide bridge between Cys49 and 167</scene> links the start of the AB loop to the N-Terminal region of helix D.  
<scene name='56/568028/Oncostatin_bridge1/1'>The disulphide bridge between Cys6 and Cys127</scene> connects the N-terminal loop (Gly4-Glu9) preceding helix A to the C terminus of helix C. <scene name='56/568028/Oncostatine_bridge2/1'>The second disulphide bridge between Cys49 and 167</scene> links the start of the AB loop to the N-Terminal region of helix D.  


The AB loop is composed of two α-helices from Pro43 to Arg46 and Glu59 to Gly64, while the residues in between pack closely and extensively against helix D. Comparatively, BC and CD loops are less stacking to the core. The BC loop located on the top of the four-helix bundle exhibits an important amount of B factors, along with several more classical secondary structures, which are a 310 helix between residues Ala95 and Asp97 followed by the α helix up to Ser101.  
The AB loop is composed of <scene name='56/568028/Abloop_residues/1'>two α-helices from Pro43 to Arg46 and Glu59 to Gly64</scene>, while the residues in between pack closely and extensively against helix D. Comparatively, BC and CD loops are less stacking to the core. The BC loop located on the top of the four-helix bundle exhibits an important amount of B factors, along with several more classical secondary structures, which are a 310 helix between residues Ala95 and Asp97 followed by the α helix up to Ser101.  




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OCA, Pierre-Yves Mocaer