Sandbox Reserved 830: Difference between revisions
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[[Image:Oncostatin structure.png|frame|left|Ribbon colored diagram of hOSM from N-terminus in blue to the C-terminus in red. The two disulphide bonds are shown as ball-and-sticks models with the sulphur atoms represented as yellow spheres. The CD loop as observed in LIF is represented by the transparent dotted section.]] [[Image:Oncostatin structure2.png|frame|right|Stereodiagram of the Cα trace for hOSM.]] | [[Image:Oncostatin structure.png|frame|left|Ribbon colored diagram of hOSM from N-terminus in blue to the C-terminus in red. The two disulphide bonds are shown as ball-and-sticks models with the sulphur atoms represented as yellow spheres. The CD loop as observed in LIF is represented by the transparent dotted section.]] [[Image:Oncostatin structure2.png|frame|right|Stereodiagram of the Cα trace for hOSM.]] | ||
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Site 3 of OSM binds to LIFR or OSMR thanks to two residues: Phe160 and Lys163, located in the N-terminal end of helix D. These amino acids are conserved in all cytokines. | Site 3 of OSM binds to LIFR or OSMR thanks to two residues: Phe160 and Lys163, located in the N-terminal end of helix D. These amino acids are conserved in all cytokines. | ||
[[Image:Osm interact osmr.png|frame|left]] [[Image:Oncostatin site3.jpg|frame|center]] | [[Image:Osm interact osmr.png|frame|left|Complimentarity between the interaction surfaces of hOSM and gp130.The solvent-accessible surfaces of site 2 on hOSM (left) and the cognate binding site on gp130 (right) are displayed with areas contributed by residues implicated in binding highlighted as coloured patches. The orientation for hOSM site 2 is rotated 90° from that in Figure 4 whereas gp130 is rotated by 180° from its orientation relative to hOSM in the putative interaction complex, as in the opening of a book.]] [[Image:Oncostatin site3.jpg|frame|center]] | ||
==Functions== | ==Functions== | ||
