Sandbox Reserved 830: Difference between revisions

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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.

[[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]]

[[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. Residues not implicated in gp130 binding are in light-blue, those with some effect are yellow, residues critical for gp130 binding are green and those critical for LIFR binding are red.]] [[Image:Oncostatin site3.jpg|frame|center]]

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@@ Line 35: / Line 35: @@
 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|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]]
+[[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. Residues not implicated in gp130 binding are in light-blue, those with some effect are yellow, residues critical for gp130 binding are green and those critical for LIFR binding are red.]] [[Image:Oncostatin site3.jpg|frame|center]]
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